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Human Metabolome Database Version 2.5

 

Showing metabocard for Pyridoxamine 5'-phosphate (HMDB01555)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-18 15:20:07
Accession Number HMDB01555
Secondary Accession Numbers Not Available
Common Name Pyridoxamine 5'-phosphate
Description Vitamin B6 is a water-soluble compound that was discovered in 1930s during nutrition studies on rats. The vitamin was named pyridoxine to indicate its structural homology to pyridine. Later it was shown that vitamin B6 could exist in two other, slightly different, chemical forms, termed pyridoxal and pyridoxamine. All three forms of vitamin B6 are precursors of an activated compound known as pyridoxal 5-phosphate (PLP), which plays a vital role as the cofactor of a large number of essential enzymes in the human body. Vitamin B6 is a water-soluble vitamin. The three major forms of vitamin B6 are pyridoxine (also known as pyridoxol), pyridoxal, and pyridoxamine, which are all converted in the liver to pyridoxal 5-phosphate (PLP) a cofactor in many reactions of amino acid metabolism. PLP also is necessary for the enzymatic reaction governing the release of glucose from glycogen.
Synonyms
  1. Pyridoxamine 5'-phosphate
  2. Pyridoxamine 5'-phosphic acid
Chemical IUPAC Name [4-(aminomethyl)-5-hydroxy-6-methyl-pyridin-3-yl]methoxyphosphonic acid
Chemical Formula C8H13N2O5P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Pyridoxals and Derivatives
Sub Class
  • Pyridoxal phosphates
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • primary amine
  • primary aliphatic amine (alkylamine)
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Vitamin B6 metabolism
Application
Source
  • Endogenous
Average Molecular Weight 248.173
Monoisotopic Molecular Weight 248.056213
Isomeric SMILES CC1=NC=C(COP(O)(O)=O)C(CN)=C1O
Canonical SMILES CC1=NC=C(COP(O)(O)=O)C(CN)=C1O
KEGG Compound ID C00647 Link Image
BioCyc ID PYRIDOXAMINE-5P Link Image
BiGG ID 35609 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01555 Link Image
Metagene Link HMDB01555 Link Image
METLIN ID Not Available
PubChem Compound 1053 Link Image
PubChem Substance 838750 Link Image
ChEBI ID 18335 Link Image
CAS Registry Number 529-96-4
InChI Identifier InChI=1/C8H13N2O5P/c1-5-8(11)7(2-9)6(3-10-5)4-15-16(12,13)14/h3,11H,2,4,9H2,1H3,(H2,12,13,14)
Synthesis Reference Katsunishi, Masatoshi; Kondo, Osamu. Pyridoxamine-5'-phosphate. Jpn. Tokkyo Koho (1972), 2 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 6.61 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.99 [Predicted by ALOGPS]; -1.8 [Predicted by PubChem via XLOGP]; -1.41 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.015 +/- 0.005 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 0.00098 +/- 0.00019 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Driskell JA, Chrisley BM, Reynolds LK, Moak SW: Plasma B6 vitamer and plasma and urinary 4-pyridoxic acid concentrations of middle-aged obese black women. J Chromatogr. 1991 Aug 23;568(2):333-40. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Vitamin B6 Metabolism SMP00017 Link Image map00750 Link Image
General References Not Available
Metabolic Enzymes
  1. Pyridoxine-5'-phosphate oxidase
  2. Pyridoxal kinase
  3. Pyridoxal phosphate phosphatase
Enzyme 1 [top]
Enzyme 1 ID 5947
Enzyme 1 Name Pyridoxine-5'-phosphate oxidase
Enzyme 1 Synonyms
  1. Pyridoxamine-phosphate oxidase
Enzyme 1 Gene Name PNPO
Enzyme 1 Protein Sequence >Pyridoxine-5'-phosphate oxidase
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVK
QFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKE
LDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPD
REYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGD
SPLGPMTHRGEEDWLYERLAP
Enzyme 1 Number of Residues 261
Enzyme 1 Molecular Weight 29987.8
Enzyme 1 Theoretical pI 7.09
Enzyme 1 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • pyridoxamine-phosphate oxidase activity
Process
  • metabolic process
  • oxidation reduction
  • pyridoxine biosynthetic process
  • pyridoxine metabolic process
  • small molecule metabolic process
  • vitamin B6 metabolic process
  • vitamin metabolic process
  • water-soluble vitamin metabolic process
Component
Enzyme 1 General Function Involved in pyridoxamine-phosphate oxidase activity
Enzyme 1 Specific Function Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 [RN:R00277]
  • (2) pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2 [RN:R00278]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NVS9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PNPO_HUMAN Link Image
Enzyme 1 PDB ID 1NRG Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >786 bp
ATGACGTGCTGGCTGCGGGGCGTCACGGCGACGTTCGGGCGACCTGCCGAGTGGCCAGGC
TACCTCAGTCACCTGTGTGGTCGCAGTGCTGCCATGGACCTGGGACCCATGCGCAAGAGT
TACCGCGGGGACCGAGAGGCATTTGAGGAGACTCATCTGACCTCCCTTGACCCAGTGAAA
CAGTTTGCTGCCTGGTTTGAGGAGGCTGTTCAGTGTCCTGACATAGGGGAAGCCAATGCC
ATGTGTCTGGCTACCTGCACCAGAGATGGAAAACCCTCTGCTCGCATGTTGCTGCTGAAG
GGCTTCGGGAAAGATGGCTTCCGCTTCTTCACTAACTTCGAGAGTCGAAAAGGAAAAGAG
CTGGACTCTAATCCCTTTGCTTCCCTTGTCTTCTACTGGGAGCCACTTAACCGTCAGGTG
CGTGTGGAAGGCCCTGTGAAGAAACTGCCTGAGGAGGAGGCTGAGTGCTACTTCCACTCC
CGCCCCAAGAGCAGCCAGATTGGGGCTGTGGTCAGCCACCAGAGTTCTGTGATCCCTGAT
CGGGAGTATCTGAGAAAGAAAAATGAGGAACTGGAACAGCTCTACCAGGATCAAGAGGTG
CCCAAGCCAAAATCCTGGGGTGGCTATGTCCTGTACCCTCAGGTGATGGAGTTCTGGCAA
GGTCAAACCAACCGCCTGCATGACCGGATAGTCTTTCGGCGGGGCCTACCCACAGGAGAT
TCCCCTTTGGGGCCCATGACCCACCGCGGGGAGGAAGACTGGCTCTATGAGAGACTTGCA
CCTTAA
Enzyme 1 GenBank Gene ID AF468030 Link Image
Enzyme 1 GeneCard ID PNPO Link Image
Enzyme 1 GenAtlas ID PNPO Link Image
Enzyme 1 HGNC ID HGNC:30260 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q21.32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  4. Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK: Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 2003 Jul;12(7):1455-63. [PubMed Link Image]
  5. Mills PB, Surtees RA, Champion MP, Beesley CE, Dalton N, Scambler PJ, Heales SJ, Briddon A, Scheimberg I, Hoffmann GF, Zschocke J, Clayton PT: Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. Hum Mol Genet. 2005 Apr 15;14(8):1077-86. Epub 2005 Mar 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6344
Enzyme 2 Name Pyridoxal kinase
Enzyme 2 Synonyms
  1. Pyridoxine kinase
Enzyme 2 Gene Name PDXK
Enzyme 2 Protein Sequence >Pyridoxal kinase
MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSD
ELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKW
DGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGP
DTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAM
LLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDI
EDPEIVVQATVL
Enzyme 2 Number of Residues 312
Enzyme 2 Molecular Weight 35102.1
Enzyme 2 Theoretical pI 6.05
Enzyme 2 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyridoxal kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
  • pyridoxine biosynthetic process
  • pyridoxine metabolic process
  • small molecule metabolic process
  • vitamin B6 metabolic process
  • vitamin metabolic process
  • water-soluble vitamin metabolic process
Component
Enzyme 2 General Function Involved in pyridoxal kinase activity
Enzyme 2 Specific Function Required for synthesis of pyridoxal-5-phosphate from vitamin B6
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + pyridoxal = ADP + pyridoxal 5'-phosphate [RN:R00174]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID O00764 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PDXK_HUMAN Link Image
Enzyme 2 PDB ID 1RFV Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >939 bp
ATGGAGGAGGAGTGCCGGGTGCTCTCCATACAGAGCCACGTCATCCGCGGCTACGTGGGC
AACCGGGCGGCCACGTTCCCGCTGCAGGTTTTGGGATTTGAGATTGACGCGGTGAACTCT
GTCCAGTTTTCAAACCACACAGGCTATGCCCACTGGAAGGGCCAAGTGCTGAATTCAGAT
GAGCTCCAGGAGTTGTACGAAGGCCTGAGGCTGAACAACATGAATAAATATGACTACGTG
CTCACAGGTTATACGAGGGACAAGTCGTTCCTGGCCATGGTGGTGGACATTGTGCAGGAG
CTGAAGCAGCAGAACCCCAGGCTGGTGTACGTGTGTGATCCAGTCTTGGGTGACAAGTGG
GACGGCGAAGGCTCGATGTACGTCCCGGAGGACCTCCTTCCCGTCTACAAAGAAAAAGTG
GTGCCGCTTGCAGACATTATCACGCCCAACCAGTTTGAGGCCGAGTTACTGAGTGGCCGG
AAGATCCACAGCCAGGAGGAAGCCTTGCGGGTGATGGACATGCTGCACTCTATGGGCCCC
GACACCGTGGTCATCACCAGCTCCGACCTGCCCTCCCCGCAGGGCAGCAACTACCTGATT
GTGCTGGGGAGTCAGAGGAGGAGGAATCCCGCTGGCTCCGTGGTGATGGAACGCATCCGG
ATGGACATTCGCAAAGTGGACGCCGTCTTTGTGGGCACTGGGGACCTGTTTGCTGCCATG
CTCCTGGCGTGGACACACAAGCACCCCAATAACCTCAAGGTGGCCTGTGAGAAGACCGTG
TCTACCTTGCACCACGTTCTGCAGAGGACCATCCAGTGTGCAAAAGCCCAGGCCGGGGAA
GGAGTGAGGCCCAGCCCCATGCAGCTGGAGCTGCGGATGGTGCAGAGCAAAAGGGACATC
GAGGACCCAGAGATCGTCGTCCAGGCCACGGTGCTGTGA
Enzyme 2 GenBank Gene ID U89606 Link Image
Enzyme 2 GeneCard ID PDXK Link Image
Enzyme 2 GenAtlas ID PDXK Link Image
Enzyme 2 HGNC ID HGNC:8819 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 21q22.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hanna MC, Turner AJ, Kirkness EF: Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of the benzodiazepine receptor. J Biol Chem. 1997 Apr 18;272(16):10756-60. [PubMed Link Image]
  2. Fang X, Zhou ZM, Lu L, Yin LL, Li JM, Zhen Y, Wang H, Sha JH: Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in human testis. Asian J Androl. 2004 Jun;6(2):83-91. [PubMed Link Image]
  3. 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 Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Lee HS, Moon BJ, Choi SY, Kwon OS: Human pyridoxal kinase: overexpression and properties of the recombinant enzyme. Mol Cells. 2000 Aug 31;10(4):452-9. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 9426
Enzyme 3 Name Pyridoxal phosphate phosphatase
Enzyme 3 Synonyms
  1. PLP phosphatase
Enzyme 3 Gene Name PDXP
Enzyme 3 Protein Sequence >Pyridoxal phosphate phosphatase
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNN
SRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRA
ELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP
WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRL
ETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED
Enzyme 3 Number of Residues 296
Enzyme 3 Molecular Weight 31697.7
Enzyme 3 Theoretical pI 6.51
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and Pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate [RN:R00173]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q96GD0 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLPP_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >891 bp
ATGGCGCGCTGCGAGAGGCTGCGCGGAGCGGCCCTGCGCGACGTGCTGGGCCGGGCGCAG
GGGGTCCTGTTCGACTGTGACGGGGTGCTGTGGAACGGCGAGCGCGCCGTGCCGGGCGCC
CCGGAGCTGCTGGAGCGGCTGGCGCGGGCCGGCAAGGCGGCTCTGTTTGTGAGCAACAAC
AGCCGGCGCGCGCGGCCCGAGCTGGCCCTGCGCTTCGCGCGCCTCGGCTTCGGGGGGCTG
CGCGCCGAGCAGCTCTTCAGCTCCGCGCTGTGCGCCGCGCGCCTGCTGCGCCAGCGCCTG
CCCGGGCCTCCGGACGCGCCGGGCGCCGTGTTCGTGCTGGGCGGCGAGGGGCTGCGCGCC
GAGCTGCGCGCCGCGGGGCTGCGCCTGGCCGGGGACCCGAGCGCGGGGGACGGCGCGGCC
CCGCGCGTGCGCGCCGTGCTTGTGGGCTACGACGAGCACTTCTCCTTCGCCAAGCTGAGG
GAGGCGTGCGCGCACCTGCGCGACCCCGAGTGCCTACTCGTGGCCACCGACCGTGACCCA
TGGCACCCGCTGAGCGACGGCAGCCGGACCCCTGGCACCGGGAGCCTGGCCGCTGCAGTG
GAGACAGCCTCGGGACGCCAGGCCCTGGTGGTGGGCAAGCCCAGCCCCTACATGTTCGAG
TGCATCACGGAGAACTTCAGCATCGACCCCGCACGCACGCTTATGGTGGGTGACCGCCTG
GAGACCGACATCCTCTTTGGCCACCGCTGCGGCATGACCACTGTGCTCACGCTCACAGGA
GTCTCCCGCCTAGAAGAGGCCCAGGCCTACCTAGCGGCCGGCCAGCACGACCTCGTGCCC
CATTACTATGTGGAGAGCATCGCAGACTTGACAGAGGGGTTGGAGGACTGA
Enzyme 3 GenBank Gene ID AY125047 Link Image
Enzyme 3 GeneCard ID PDXP Link Image
Enzyme 3 GenAtlas ID PDXP Link Image
Enzyme 3 HGNC ID HGNC:30259 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 22cen-q12.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, Kwon OS: Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J Biol Chem. 2003 Dec 12;278(50):50040-6. Epub 2003 Sep 30. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
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Enzyme 3 Metabolite References Not Available