|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6009 |
| Enzyme 1 Name |
6-phosphofructokinase type C |
| Enzyme 1 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme C
- PFK-C
- 6- phosphofructokinase, platelet type
|
| Enzyme 1 Gene Name |
PFKP |
| Enzyme 1 Protein Sequence |
>6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
|
| Enzyme 1 Number of Residues |
784 |
| Enzyme 1 Molecular Weight |
85597 |
| Enzyme 1 Theoretical pI |
7.60 |
| Enzyme 1 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 1 General Function |
Carbohydrate transport and metabolism |
| Enzyme 1 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
560105  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q01813  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
K6PP_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
|
| Enzyme 1 GenBank Gene ID |
D25328  |
| Enzyme 1 GeneCard ID |
PFKP  |
| Enzyme 1 GenAtlas ID |
PFKP  |
| Enzyme 1 HGNC ID |
HGNC:8878  |
| Enzyme 1 Chromosome Location |
10 |
| Enzyme 1 Locus |
10p15.3-p15.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed
]
- Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6033 |
| Enzyme 2 Name |
6-phosphofructokinase, liver type |
| Enzyme 2 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme B
- PFK-B
|
| Enzyme 2 Gene Name |
PFKL |
| Enzyme 2 Protein Sequence |
>6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
|
| Enzyme 2 Number of Residues |
780 |
| Enzyme 2 Molecular Weight |
85020 |
| Enzyme 2 Theoretical pI |
7.54 |
| Enzyme 2 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 2 General Function |
Carbohydrate transport and metabolism |
| Enzyme 2 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
35431  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P17858  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
K6PL_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
|
| Enzyme 2 GenBank Gene ID |
X15573  |
| Enzyme 2 GeneCard ID |
PFKL  |
| Enzyme 2 GenAtlas ID |
PFKL  |
| Enzyme 2 HGNC ID |
HGNC:8876  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed
]
- Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6037 |
| Enzyme 3 Name |
6-phosphofructokinase, muscle type |
| Enzyme 3 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme A
- PFK-A
- Phosphofructokinase-M
|
| Enzyme 3 Gene Name |
PFKM |
| Enzyme 3 Protein Sequence |
>6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
|
| Enzyme 3 Number of Residues |
780 |
| Enzyme 3 Molecular Weight |
85184 |
| Enzyme 3 Theoretical pI |
8.07 |
| Enzyme 3 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 3 General Function |
Carbohydrate transport and metabolism |
| Enzyme 3 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1101758  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P08237  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
K6PF_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
|
| Enzyme 3 GenBank Gene ID |
M59741  |
| Enzyme 3 GeneCard ID |
PFKM  |
| Enzyme 3 GenAtlas ID |
PFKM  |
| Enzyme 3 HGNC ID |
HGNC:8877  |
| Enzyme 3 Chromosome Location |
12 |
| Enzyme 3 Locus |
12q13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed
]
- Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed
]
- Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed
]
- Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed
]
- Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed
]
- Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed
]
- Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed
]
- Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed
]
- Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6039 |
| Enzyme 4 Name |
Pyruvate kinase isozymes M1/M2 |
| Enzyme 4 Synonyms |
- Pyruvate kinase muscle isozyme
- Pyruvate kinase 2/3
- Cytosolic thyroid hormone-binding protein
- CTHBP
- THBP1
|
| Enzyme 4 Gene Name |
PKM2 |
| Enzyme 4 Protein Sequence |
>Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
|
| Enzyme 4 Number of Residues |
531 |
| Enzyme 4 Molecular Weight |
57938 |
| Enzyme 4 Theoretical pI |
7.94 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Carbohydrate transport and metabolism |
| Enzyme 4 Specific Function |
ATP + pyruvate = ADP + phosphoenolpyruvate |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
189998  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P14618  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
KPYM_HUMAN  |
| Enzyme 4 PDB ID |
1F3X  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGAACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
|
| Enzyme 4 GenBank Gene ID |
M23725  |
| Enzyme 4 GeneCard ID |
PKM2  |
| Enzyme 4 GenAtlas ID |
PKM2  |
| Enzyme 4 HGNC ID |
HGNC:9021  |
| Enzyme 4 Chromosome Location |
15 |
| Enzyme 4 Locus |
15q22 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed
]
- Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed
]
- Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6041 |
| Enzyme 5 Name |
Pyruvate kinase isozymes R/L |
| Enzyme 5 Synonyms |
- R-type/L-type pyruvate kinase
- Red cell/liver pyruvate kinase
- Pyruvate kinase 1
|
| Enzyme 5 Gene Name |
PKLR |
| Enzyme 5 Protein Sequence |
>Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
|
| Enzyme 5 Number of Residues |
574 |
| Enzyme 5 Molecular Weight |
61831 |
| Enzyme 5 Theoretical pI |
7.83 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Carbohydrate transport and metabolism |
| Enzyme 5 Specific Function |
ATP + pyruvate = ADP + phosphoenolpyruvate |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
3327365  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P30613  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
KPYR_HUMAN  |
| Enzyme 5 PDB ID |
1LIU  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
|
| Enzyme 5 GenBank Gene ID |
AB015983  |
| Enzyme 5 GeneCard ID |
PKLR  |
| Enzyme 5 GenAtlas ID |
PKLR  |
| Enzyme 5 HGNC ID |
HGNC:9020  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
1q21 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed
]
- Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed
]
- Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed
]
- Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed
]
- Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed
]
- Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed
]
- Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed
]
- Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed
]
- Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed
]
- Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed
]
- Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed
]
- Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed
]
- Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed
]
- Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed
]
- Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed
]
- Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed
]
- Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed
]
- Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6174 |
| Enzyme 6 Name |
Phosphoenolpyruvate carboxykinase, cytosolic [GTP] |
| Enzyme 6 Synonyms |
- Phosphoenolpyruvate carboxylase
- PEPCK-C
|
| Enzyme 6 Gene Name |
PCK1 |
| Enzyme 6 Protein Sequence |
>Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQM
EEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEE
DFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPV
LEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSL
PGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNV
AETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAW
ESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPF
AMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWM
FNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQV
NADLPCEIEREILALKQRISQM
|
| Enzyme 6 Number of Residues |
622 |
| Enzyme 6 Molecular Weight |
69195 |
| Enzyme 6 Theoretical pI |
6.05 |
| Enzyme 6 GO Classification |
| Function |
- GTP binding
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- guanyl nucleotide binding
- lyase activity
- nucleotide binding
- phosphoenolpyruvate carboxykinase activity
- purine nucleotide binding
|
| Process |
- alcohol metabolism
- cellular metabolism
- gluconeogenesis
- glucose metabolism
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Energy production and conversion |
| Enzyme 6 Specific Function |
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2) |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
189945  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P35558  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PPCKC_HUMAN  |
| Enzyme 6 PDB ID |
1NHX  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1869 bp
ATGCCTCCTCAGCTGCAAAACGGCCTGAACCTCTCGGCCAAAGTTGTCCAGGGAAGCCTG
GACAGCCTGCCCCAGGCAGTGAGGGAGTTTCTCGAGAATAACGCTGAGCTGTGTCAGCCT
GATCACATCCACATCTGTGACGGCTCTGAGGAGGAGAATGGGCGGCTTCTGGGCCAGATG
GAGGAAGAGGGCATCCTCAGGCGGCTGAAGAAGTATGACAACTGCTGGTTGGCTCTCACT
GACCCCAGGGATGTGGCCAGGATCGAAAGCAAGACGGTTATCGTCACCCAAGAGCAAAGA
GACACAGTGCCCATCCCCAAAACAGGCCTCAGCCAGCTCGGTCGCTGGATGTCAGAGGAG
GATTTTGAGAAAGCGTTCAATGCCAGGTTCCCAGGGTGCATGAAAGGTCGCACCATGTAC
GTCATCCCATTCAGCATGGGGCCGCTGGGCTCACCTCTGTCGAAGATCGGCATCGAGCTG
ACGGATTCGCCCTACGTGGTGGCCAGCATGCGGATCATGACGCGGATGGGCACGCCCGTC
CTGGAAGCACTGGGCGATGGGGAGTTTGTCAAATGCCTCCATTCTGTGGGGTGCCCTCTG
CCTTTACAAAAGCCTTTGGTCAACAACTGGCCCTGCAACCCGGAGCTGACGCTCATCGCC
CACCTGCCTGACCGCAGAGAGATCATCTCCTTTGGCAGTGGGTACGGCGGGAACTCGCTG
CTCGGGAAGAAGTGCTTTGCTCTCAGGATGGCCAGCCGGCTGGCAGAGGAGGAAGGGTGG
CTGGCAGAGCACATGCTGATTCTGGGTATAACCAACCCTGAGGGTGAGAAGAAGTACCTG
GCGGCCGCATTTCCCAGCGCCTGCGGGAAGACCAACCTGGCCATGATGAACCCCAGCCTC
CCCGGGTGGAAGGTTGAGTGCGTCGGGGATGACATTGCCTGGATGAAGTTTGACGCACAA
GGTCATTTAAGGGCCATCAACCCAGAAAATGGCTTTTTCGGTGTCGCTCCTGGGACTTCA
GTGAAGACCAACCCCAATGCCATCAAGACCATCCAGAAGAACACAATCTTTACCAATGTG
GCCGAGACCAGCGACGGGGGCGTTTACTGGGAAGGCATTGATGAGCCGCTAGCTTCAGGC
GTCACCATCACGTCCTGGAAGAATAAGGAGTGGAGCTCAGAGGATGGGGAACCTTGTGCC
CACCCCAACTCGAGGTTCTGCACCCCTGCCAGCCAGTGCCCCATCATTGATGCTGCCTGG
GAGTCTCCGGAAGGTGTTCCCATTGAAGGCATTATCTTTGGAGGCCGTAGACCTGCTGGT
GTCCCTCTAGTCTATGAAGCTCTCAGCTGGCAACATGGAGTCTTTGTGGGGGCGGCCATG
AGATCAGAGGCCACAGCGGCTGCAGAACATAAAGGCAAAATCATCATGCATGACCCCTTT
GCCATGCGGCCCTTCTTTGGCTACAACTTCGGCAAATACCTGGCCCACTGGCTTAGCATG
GCCCAGCACCCAGCAGCCAAACTGCCCAAGATCTTCCATGTCAACTGGTTCCGGAAGGAC
AAGGAAGGCAAATTCCTCTGGCCAGGCTTTGGAGAGAACTCCAGGGTGCTGGAGTGGATG
TTCAACCGGATCGATGGAAAAGCCAGCACCAACGTCACGCCCATAGGCTACATCCCCAAG
GAGGATGCCCTGAACCTGAAAGGCCTGGGGCACATCAACATGATGGAGCTTTTCAGCATC
TCCAAGGAATTCTGGGACAAGGAGGTGGAAGACATCGAGAAGTATCTGGTGGATCAAGTC
AATGCCGACCTCCCCTGTGAAATCGAGAGAGAGATCCTTGCCTTGAAGCAAAGAATAAGC
CAGATGTAA
|
| Enzyme 6 GenBank Gene ID |
L05144  |
| Enzyme 6 GeneCard ID |
PCK1  |
| Enzyme 6 GenAtlas ID |
PCK1  |
| Enzyme 6 HGNC ID |
HGNC:8724  |
| Enzyme 6 Chromosome Location |
20 |
| Enzyme 6 Locus |
20q13.31 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Stoffel M, Xiang KS, Espinosa R 3rd, Cox NJ, Le Beau MM, Bell GI: cDNA sequence and localization of polymorphic human cytosolic phosphoenolpyruvate carboxykinase gene (PCK1) to chromosome 20, band q13.31: PCK1 is not tightly linked to maturity-onset diabetes of the young. Hum Mol Genet. 1993 Jan;2(1):1-4. [PubMed
]
- Ting CN, Burgess DL, Chamberlain JS, Keith TP, Falls K, Meisler MH: Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20. Genomics. 1993 Jun;16(3):698-706. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- O'Brien RM, Printz RL, Halmi N, Tiesinga JJ, Granner DK: Structural and functional analysis of the human phosphoenolpyruvate carboxykinase gene promoter. Biochim Biophys Acta. 1995 Dec 27;1264(3):284-8. [PubMed
]
- Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ: Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J Mol Biol. 2002 Feb 15;316(2):257-64. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6374 |
| Enzyme 7 Name |
Beta-enolase |
| Enzyme 7 Synonyms |
- 2-phospho-D-glycerate hydro-lyase
- Muscle-specific enolase
- MSE
- Skeletal muscle enolase
- Enolase 3
|
| Enzyme 7 Gene Name |
ENO3 |
| Enzyme 7 Protein Sequence |
>Beta-enolase
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGK
GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCK
AGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKE
AMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKV
VIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDD
WATWTSFLSGVNIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLA
QSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDK
AIFAGRKFRNPKAK
|
| Enzyme 7 Number of Residues |
434 |
| Enzyme 7 Molecular Weight |
46987 |
| Enzyme 7 Theoretical pI |
7.84 |
| Enzyme 7 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- phosphopyruvate hydratase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- phosphopyruvate hydratase complex
- protein complex
|
|
| Enzyme 7 General Function |
Carbohydrate transport and metabolism |
| Enzyme 7 Specific Function |
Appears to have a function in striated muscle development and regeneration |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
31170  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P13929  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
ENOB_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1305 bp
ATGGCCATGCAGAAAATCTTTGCCCGGGAAATCTTGGACTCCAGGGGCAACCCCACGGTG
GAGGTGGACCTGCACACGGCCAAGGGCCGATTCCGAGCAGCTGTGCCCAGTGGGGCTTCC
ACGGGTATCTATGAGGCTCTGGAACTAAGAGACGGAGACAAAGGCCGCTACCTGGGGAAA
GGAGTCCTGAAGGCTGTGGAGAACATCAACAATACTCTGGGCCCTGCTCTGCTGCAAAAG
AAACTAAGCGTTGTTGATCAAGAAAAAGTTGACAAATTTATGATTGAGCTAGATGGGACC
GAGAATAAGTCCAAGTTTGGGGCCAATGCCATCCTGGGCGTGTCCTTGGCCGTGTGTAAG
GCGGGAGCAGCTGAGAAGGGGGTCCCCCTGTACCGCCACATCGCAGATCTCGCTGGGAAC
CCTGACCTCATACTCCCAGTGCCAGCCTTCAATGTGATCAACGGGGGCTCCCATGCTGGA
AACAACTTGGCCATGCAGGAGTTCATGATTCTGCCTGTGGGAGCCAGCTCCTTCAAGGAA
GCCATGCGCATTGGCGCCGAGGTCTACCACCACCTCAAGGGGGTCATCAAGGCCAAGTAT
GGGAAGGATGCCACCAATGTGGGTGATGAAGGTGGCTTCGCACCCAACATCCTGGAGAAC
AATGAGGCCCTGGAGCTGCTGAAGACGGCCATCCAGGCGGCTGGTTACCCAGACAAGGTG
GTGATCGGCATGGATGTGGCAGCATCTGAGTTCTATCGCAATGGGAAGTACGATCTTGAC
TTCAAGTCGCCTGATGATCCCGCACGGCACATCACTGGGGAGAAGCTCGGAGAGCTGTAT
AAGAGCTTTATCAAGAACTATCCTGTGGTCTCCATCGAAGACCCCTTTGACCAGGATGAC
TGGGCCACTTGGACCTCCTTCCTCTCGGGGGTGAACATCCAGATTGTGGGGGATGACTTG
ACAGTCACCAACCCCAAGAGGATTGCCCAGGCCGTTGAGAAGAAGGCCTGCAACTGTCTG
CTGCTGAAGGTCAACCAGATCGGCTCGGTGACCGAATCGATCCAGGCGTGCAAACTGGCT
CAGTCTAATGGCTGGGGGGTGATGGTGAGCCACCGCTCAGGGGAGACTGAGGACACATTC
ATTGCTGACCTTGTGGTGGGGCTCTGCACAGGACAGATCAAGACTGGCGCCCCCTGCCGC
TCGGAGCGTCTGGCCAAATACAACCAACTCATGAGGATCGAGGAGGCTCTTGGGGACAAG
GCAATCTTTGCTGGACGCAAGTTCCGTAACCCGAAGGCCAAGTGA
|
| Enzyme 7 GenBank Gene ID |
X16504  |
| Enzyme 7 GeneCard ID |
ENO3  |
| Enzyme 7 GenAtlas ID |
ENO3  |
| Enzyme 7 HGNC ID |
HGNC:3354  |
| Enzyme 7 Chromosome Location |
17 |
| Enzyme 7 Locus |
17pter-p11 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Peshavaria M, Hinks LJ, Day IN: Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone. Nucleic Acids Res. 1989 Nov 11;17(21):8862. [PubMed
]
- Peshavaria M, Day IN: Molecular structure of the human muscle-specific enolase gene (ENO3). Biochem J. 1991 Apr 15;275 ( Pt 2):427-33. [PubMed
]
- Cali L, Feo S, Oliva D, Giallongo A: Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE). Nucleic Acids Res. 1990 Apr 11;18(7):1893. [PubMed
]
- Giallongo A, Venturella S, Oliva D, Barbieri G, Rubino P, Feo S: Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA. Eur J Biochem. 1993 Jun 1;214(2):367-74. [PubMed
]
- Comi GP, Fortunato F, Lucchiari S, Bordoni A, Prelle A, Jann S, Keller A, Ciscato P, Galbiati S, Chiveri L, Torrente Y, Scarlato G, Bresolin N: Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis. Ann Neurol. 2001 Aug;50(2):202-7. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6375 |
| Enzyme 8 Name |
Gamma-enolase |
| Enzyme 8 Synonyms |
- 2-phospho-D-glycerate hydro-lyase
- Neural enolase
- Neuron-specific enolase
- NSE
- Enolase 2
|
| Enzyme 8 Gene Name |
ENO2 |
| Enzyme 8 Protein Sequence |
>Gamma-enolase
MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGK
GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCK
AGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRD
AMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKI
VIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDD
WAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLA
QENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDE
ARFAGHNFRNPSVL
|
| Enzyme 8 Number of Residues |
434 |
| Enzyme 8 Molecular Weight |
47269 |
| Enzyme 8 Theoretical pI |
4.65 |
| Enzyme 8 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- phosphopyruvate hydratase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- phosphopyruvate hydratase complex
- protein complex
|
|
| Enzyme 8 General Function |
Carbohydrate transport and metabolism |
| Enzyme 8 Specific Function |
Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
930063  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P09104  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ENOG_HUMAN  |
| Enzyme 8 PDB ID |
1TE6  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1299 bp
TCCATACAGAAGATCTGGGCCCGGGAGATCCTGGACTCCCGTGGGAACCCCACAGTGGAG
GTGGATCTCTATACTGCCAAAGGTCTTTTCCGGGCTGCAGTGCCCAGTGGAGCCTCTACG
GGCATCTATGAGGCCCTGGAGCTGAGGGATGGAGACAAACAGCGTTACTTAGGCAAAGGT
GTCCTGAAGGCAGTGGACCACATCAACTCCACCATCGCGCCAGCCCTCATCAGCTCAGGT
CTCTCTGTGGTGGAGCAAGAGAAGCTGGACAACCTGATGCTGGAGTTGGATGGGACTGAG
AACAAATCCAAGTTTGGGGCCAATGCCATCCTGGGTGTGTCTCTGGCCGTGTGTAAGGCA
GGGGCAGCTGAGCGGGAACTGCCCCTGTATCGCCACATTGCTCAGCTGGCCGGGAACTCA
GACCTCATCCTGCCTGTGCCGGCCTTCAACGTGATCAATGGTGGCTCTCATGCTGGCAAC
AAGCTGGCCATGCAGGAGTTCATGATCCTCCCAGTGGGAGCTGAGAGCTTTCGGGATGCC
ATGCGACTAGGTGCAGAGGTCTACCATACTCTCAAGGGAGTCATCAAGGACAAATACGGC
AAGGATGCCACCAATGTGGGGGATGAAGGTGGCTTTGCCCCCAATATCCTGGAGAACAGT
GAAGCCTTGGAGCTGGTTAAGGAAGCCATCGACAAGGCTGGCTACACGGAAAAAATGGTT
ATTGGCATGGATGTTGCTGCCTCAGAGTTTTATCGTGATGGCAAATATGACTTGGACTTC
AAGTCTCCCACTGATCCTTCCCGATACATCACTGGGGACCAGCTGGGGGCACTCTACCAG
GACTTTGTCAGGGACTATCCTGTGGTCTCCATTGAGGACCCATTTGACCAGGATGATTGG
GCTGCCTGGTCCAAGTTCACAGCCAATGTAGGGATCCAGATTGTGGGTGATGACCTGACA
GTGACCAACCCAAAACGTATTGAGCGGGCAGTGGAAGAAAAGGCCTGCAACTGTCTGCTG
CTCAAGGTCAACCAGATCGGCTCGGTCACTGAAGCCATCCAAGCGTGCAAGCTGGCCCAG
GAGAATGGCTGGGGGGTCATGGTGAGTCATCGCTCAGGAGAGACTGAGGACACATTCATT
GCTGACCTGGTGGTGGGGCTGTGCACAGGCCAGATCAAGACTGGTGCCCCGTGCCGTTCT
GAACGTCTGGCTAAATACAATCAGCTCATGAGAATTGAGGAAGAGCTGGGGGATGAAGCT
CGCTTTGCCGGACATAACTTCCGTAATCCCAGTGTGCTG
|
| Enzyme 8 GenBank Gene ID |
X13120  |
| Enzyme 8 GeneCard ID |
ENO2  |
| Enzyme 8 GenAtlas ID |
ENO2  |
| Enzyme 8 HGNC ID |
HGNC:3353  |
| Enzyme 8 Chromosome Location |
12 |
| Enzyme 8 Locus |
12p13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- McAleese SM, Dunbar B, Fothergill JE, Hinks LJ, Day IN: Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE). Eur J Biochem. 1988 Dec 15;178(2):413-7. [PubMed
]
- Oliva D, Barba G, Barbieri G, Giallongo A, Feo S: Cloning, expression and sequence homologies of cDNA for human gamma enolase. Gene. 1989 Jul 15;79(2):355-60. [PubMed
]
- Van Obberghen E, Kamholz J, Bishop JG 3rd, Zomzely-Neurath C, Lazzarini RA, Lazzarini RA: Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin. J Neurosci Res. 1988 Apr;19(4):450-6. [PubMed
]
- Oliva D, Cali L, Feo S, Giallongo A: Complete structure of the human gene encoding neuron-specific enolase. Genomics. 1991 May;10(1):157-65. [PubMed
]
- Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed
]
- Day IN, Allsopp MT, Moore DC, Thompson RJ: Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs. FEBS Lett. 1987 Sep 28;222(1):139-43. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6376 |
| Enzyme 9 Name |
Alpha-enolase |
| Enzyme 9 Synonyms |
- 2-phospho-D-glycerate hydro-lyase
- Non- neural enolase
- NNE
- Enolase 1
- Phosphopyruvate hydratase
- C-myc promoter-binding protein
- MBP-1
- MPB-1
- Plasminogen-binding protein
|
| Enzyme 9 Gene Name |
ENO1 |
| Enzyme 9 Protein Sequence |
>Alpha-enolase
MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGK
GVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCK
AGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFRE
AMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKV
VIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDD
WGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLA
QANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSK
AKFAGRNFRNPLAK
|
| Enzyme 9 Number of Residues |
434 |
| Enzyme 9 Molecular Weight |
47169 |
| Enzyme 9 Theoretical pI |
7.46 |
| Enzyme 9 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- phosphopyruvate hydratase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- phosphopyruvate hydratase complex
- protein complex
|
|
| Enzyme 9 General Function |
Carbohydrate transport and metabolism |
| Enzyme 9 Specific Function |
MBP1 binds to the c-myc promoter and acts as a transcriptional repressor. May be a tumor suppressor |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
182114  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P06733  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
ENOA_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1305 bp
ATGTCTATTCTCAAGATCCATGCCAGGGAGATCTTTGACTCTCGCGGGAATCCCACTGTT
GAGGTTGATCTCTTCACCTCAAAAGGTCTCTTCAGAGCTGCTGTGCCCAGTGGTGCTTCA
ACTGGTATCTATGAGGCCCTAGAGCTCCGGGACAATGATAAGACTCGCTATATGGGGAAG
GGTGTCTCAAAGGCTGTTGAGCACATCAATAAAACTATTGCGCCTGCCCTGGTTAGCAAG
AAACTGAACGTCACAGAACAAGAGAAGATTGACAAACTGATGATCGAGATGGATGGAACA
GAAAATAAATCTAAGTTTGGTGCGAACGCCATTCTGGGGGTGTCCCTTGCCGTCTGCAAA
GCTGGTGCCGTTGAGAAGGGGGTCCCCCTGTACCGCCACATCGCTGACTTGGCTGGCAAC
TCTGAAGTCATCCTGCCAGTCCCGGCGTTCAATGTCATCAATGGCGGTTCTCATGCTGGC
AACAAGCTGGCCATGCAGGAGTTCATGATCCTCCCAGTCGGTGCAGCAAACTTCAGGGAA
GCCATGCGCATTGGAGCAGAGGTTTACCACAACCTGAAGAATGTCATCAAGGAGAAATAT
GGGAAAGATGCCACCAATGTGGGGGATGAAGGCGGGTTTGCTCCCAACATCCTGGAGAAT
AAAGAAGGCCTGGAGCTGCTGAAGACTGCTATTGGGAAAGCTGGCTACACTGATAAGGTG
GTCATCGGCATGGACGTAGCGGCCTCCGAGTTCTTCAGGTCTGGGAAGTATGACCTGGAC
TTCAAGTCTCCCGATGACCCCAGCAGGTACATCTCGCCTGACCAGCTGGCTGACCTGTAC
AAGTCCTTCATCAAGGACTACCCAGTGGTGTCTATCGAAGATCCCTTTGACCAGGATGAC
TGGGGAGCTTGGCAGAAGTTCACAGCCAGTGCAGGAATCCAGGTAGTGGGGGATGATCTC
ACAGTGACCAACCCAAAGAGGATCGCCAAGGCCGTGAACGAGAAGTCCTGCAACTGCCTC
CTGCTCAAAGTCAACCAGATTGGCTCCGTGACCGAGTCTCTTCAGGCGTGCAAGCTGGCC
CAGGCCAATGGTTGGGGCGTCATGGTGTCTCATCGTTCGGGGGAGACTGAAGATACCTTC
ATCGCTGACCTGGTTGTGGGGCTGTGCACTGGGCAGATCAAGACTGGTGCCCCTTGCCGA
TCTGAGCGCTTGGCCAAGTACAACCAGCTCCTCAGAATTGAAGAGGAGCTGGGCAGCAAG
GCTAAGTTTGCCGGCAGGAACTTCAGAAACCCCTTGGCCAAGTAA
|
| Enzyme 9 GenBank Gene ID |
M14328  |
| Enzyme 9 GeneCard ID |
ENO1  |
| Enzyme 9 GenAtlas ID |
ENO1  |
| Enzyme 9 HGNC ID |
HGNC:3350  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.3-p36.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Giallongo A, Feo S, Moore R, Croce CM, Showe LC: Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6741-5. [PubMed
]
- Giallongo A, Oliva D, Cali L, Barba G, Barbieri G, Feo S: Structure of the human gene for alpha-enolase. Eur J Biochem. 1990 Jul 5;190(3):567-73. [PubMed
]
- Ray R, Miller DM: Cloning and characterization of a human c-myc promoter-binding protein. Mol Cell Biol. 1991 Apr;11(4):2154-61. [PubMed
]
- Walter M, Berg H, Leidenberger FA, Schweppe KW, Northemann W: Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis. J Autoimmun. 1995 Dec;8(6):931-45. [PubMed
]
- Onyango P, Lubyova B, Gardellin P, Kurzbauer R, Weith A: Molecular cloning and expression analysis of five novel genes in chromosome 1p36. Genomics. 1998 Jun 1;50(2):187-98. [PubMed
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
- Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed
]
- Mohammad RM, Hamdan MY, al-Katib A: Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma. Enzyme Protein. 1994-1995;48(1):37-44. [PubMed
]
- Ghosh AK, Steele R, Ray RB: Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. Mol Cell Biol. 1999 Apr;19(4):2880-6. [PubMed
]
- Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A: ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett. 2000 May 4;473(1):47-52. [PubMed
]
- Lopez-Alemany R, Longstaff C, Hawley S, Mirshahi M, Fabregas P, Jardi M, Merton E, Miles LA, Felez J: Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-Enolase. Am J Hematol. 2003 Apr;72(4):234-42. [PubMed
]
- Arza B, Felez J, Lopez-Alemany R, Miles LA, Munoz-Canoves P: Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display. Thromb Haemost. 1997 Sep;78(3):1097-103. [PubMed
]
- Adamus G, Amundson D, Seigel GM, Machnicki M: Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells. J Autoimmun. 1998 Dec;11(6):671-7. [PubMed
]
- Subramanian A, Miller DM: Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. J Biol Chem. 2000 Feb 25;275(8):5958-65. [PubMed
]
- Pancholi V: Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci. 2001 Jun;58(7):902-20. [PubMed
]
- Ghosh AK, Majumder M, Steele R, White RA, Ray RB: A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1. Mol Cell Biol. 2001 Jan;21(2):655-62. [PubMed
]
- Ochi H, Horiuchi I, Araki N, Toda T, Araki T, Sato K, Murai H, Osoegawa M, Yamada T, Okamura K, Ogino T, Mizumoto K, Yamashita H, Saya H, Kira J: Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy. FEBS Lett. 2002 Sep 25;528(1-3):197-202. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
16476 |
| Enzyme 10 Name |
cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e) |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
PKM2 |
| Enzyme 10 Protein Sequence |
>cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
|
| Enzyme 10 Number of Residues |
531 |
| Enzyme 10 Molecular Weight |
57938 |
| Enzyme 10 Theoretical pI |
7.94 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Carbohydrate transport and metabolism |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
B2R5N8  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
B2R5N8_HUMAN  |
| Enzyme 10 PDB ID |
1F3X  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
Not Available |
| Enzyme 10 GenBank Gene ID |
AK312253  |
| Enzyme 10 GeneCard ID |
B2R5N8  |
| Enzyme 10 GenAtlas ID |
Not Available |
| Enzyme 10 HGNC ID |
Not Available |
| Enzyme 10 Chromosome Location |
15 |
| Enzyme 10 Locus |
15q22 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
16530 |
| Enzyme 11 Name |
cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b) |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
NANS |
| Enzyme 11 Protein Sequence |
>cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b)
MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAKECGADCAKFQKSELEF
KFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVE
FLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFC
FLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVALGAKVLERHIT
LDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQLLPCEMACNEKLGKSVVAKVK
IPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKKVLVTVEEDDTIMEELVDNHGKKIKS
|
| Enzyme 11 Number of Residues |
359 |
| Enzyme 11 Molecular Weight |
40308 |
| Enzyme 11 Theoretical pI |
6.73 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
Not Available |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
B2RE98  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
B2RE98_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
Not Available |
| Enzyme 11 GenBank Gene ID |
AK316608  |
| Enzyme 11 GeneCard ID |
B2RE98  |
| Enzyme 11 GenAtlas ID |
Not Available |
| Enzyme 11 HGNC ID |
Not Available |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
Not Available |
| Enzyme 11 Metabolite References |
Not Available |