|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5742 |
| Enzyme 1 Name |
11-cis retinol dehydrogenase |
| Enzyme 1 Synonyms |
- 11-cis RDH
|
| Enzyme 1 Gene Name |
RDH5 |
| Enzyme 1 Protein Sequence |
>11-cis retinol dehydrogenase
MWLPLLLGALLWAVLWLLRDRQSLPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCL
TPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFGLVNNAGVAGIIGP
TPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGGYCVSKF
GLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQAHYGGA
FLTKYLKMQQRIMNLICDPDLTKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPAS
LVDAVLTWVLPKPAQAVY
|
| Enzyme 1 Number of Residues |
318 |
| Enzyme 1 Molecular Weight |
34978.4 |
| Enzyme 1 Theoretical pI |
9.70 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Active in the presence of NAD as cofactor but not in the presence of NADP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- retinol + NAD+ = retinal + NADH + H+ [RN:R02124]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q92781  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
RDH1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>957 bp
ATGTGGCTGCCTCTTCTGCTGGGTGCCTTACTCTGGGCAGTGCTGTGGTTGCTCAGGGAC
CGGCAGAGCCTGCCCGCCAGCAATGCCTTTGTCTTCATCACCGGCTGTGACTCAGGCTTT
GGGCGCCTTCTGGCACTGCAGCTGGACCAGAGAGGCTTCCGAGTCCTGGCCAGCTGCCTG
ACCCCCTCCGGGGCCGAGGACCTGCAGCGGGTGGCCTCCTCCCGCCTCCACACCACCCTG
TTGGATATCACTGATCCCCAGAGCGTCCAGCAGGCAGCCAAGTGGGTGGAGATGCACGTT
AAGGAAGCAGGGCTTTTTGGTCTGGTGAATAATGCTGGTGTGGCTGGTATCATCGGACCC
ACACCATGGCTGACCCGGGACGATTTCCAGCGGGTGCTGAATGTGAACACAATGGGTCCC
ATCGGGGTCACCCTTGCCCTGCTGCCTCTGCTGCAGCAAGCCCGGGGCCGGGTGATCAAC
ATCACCAGCGTCCTGGGTCGCCTGGCAGCCAATGGTGGGGGCTACTGTGTCTCCAAATTT
GGCCTGGAGGCCTTCTCTGACAGCCTGAGGCGGGATGTAGCTCATTTTGGGATACGAGTC
TCCATCGTGGAGCCTGGCTTCTTCCGAACCCCTGTGACCAACCTGGAGAGTCTGGAGAAA
ACCCTGCAGGCCTGCTGGGCACGGCTGCCTCCTGCCACACAGGCCCACTATGGGGGGGCC
TTCCTCACCAAGTACCTGAAAATGCAACAGCGCATCATGAACCTGATCTGTGACCCGGAC
CTAACCAAGGTGAGCCGATGCCTGGAGCATGCCCTGACTGCTCGACACCCCCGAACCCGC
TACAGCCCAGGTTGGGATGCCAAGCTGCTCTGGCTGCCTGCCTCCTACCTGCCAGCCAGC
CTGGTGGATGCTGTGCTCACCTGGGTCCTTCCCAAGCCTGCCCAAGCAGTCTACTGA
|
| Enzyme 1 GenBank Gene ID |
U43559  |
| Enzyme 1 GeneCard ID |
RDH5  |
| Enzyme 1 GenAtlas ID |
RDH5  |
| Enzyme 1 HGNC ID |
HGNC:9940  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
12q13-q14 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Simon A, Lagercrantz J, Bajalica-Lagercrantz S, Eriksson U: Primary structure of human 11-cis retinol dehydrogenase and organization and chromosomal localization of the corresponding gene. Genomics. 1996 Sep 15;36(3):424-30. [PubMed
]
- 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
]
- Gonzalez-Fernandez F, Kurz D, Bao Y, Newman S, Conway BP, Young JE, Han DP, Khani SC: 11-cis retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus. Mol Vis. 1999 Dec 30;5:41. [PubMed
]
- Yamamoto H, Simon A, Eriksson U, Harris E, Berson EL, Dryja TP: Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus. Nat Genet. 1999 Jun;22(2):188-91. [PubMed
]
- Kuroiwa S, Kikuchi T, Yoshimura N: A novel compound heterozygous mutation in the RDH5 gene in a patient with fundus albipunctatus. Am J Ophthalmol. 2000 Nov;130(5):672-5. [PubMed
]
- Nakamura M, Hotta Y, Tanikawa A, Terasaki H, Miyake Y: A high association with cone dystrophy in Fundus albipunctatus caused by mutations of the RDH5 gene. Invest Ophthalmol Vis Sci. 2000 Nov;41(12):3925-32. [PubMed
]
- Driessen CA, Janssen BP, Winkens HJ, Kuhlmann LD, Van Vugt AH, Pinckers AJ, Deutman AF, Janssen JJ: Null mutation in the human 11-cis retinol dehydrogenase gene associated with fundus albipunctatus. Ophthalmology. 2001 Aug;108(8):1479-84. [PubMed
]
- Hotta K, Nakamura M, Kondo M, Ito S, Terasaki H, Miyake Y, Hida T: Macular dystrophy in a Japanese family with fundus albipunctatus. Am J Ophthalmol. 2003 Jun;135(6):917-9. [PubMed
]
- Yamamoto H, Yakushijin K, Kusuhara S, Escano MF, Nagai A, Negi A: A novel RDH5 gene mutation in a patient with fundus albipunctatus presenting with macular atrophy and fading white dots. Am J Ophthalmol. 2003 Sep;136(3):572-4. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
12897 |
| Enzyme 2 Name |
Acyl-CoA wax alcohol acyltransferase 1 |
| Enzyme 2 Synonyms |
- Diacylglycerol O-acyltransferase 2-like protein 3
- Diacylglycerol acyltransferase 2
- Long-chain-alcohol O-fatty-acyltransferase 1
|
| Enzyme 2 Gene Name |
AWAT1 |
| Enzyme 2 Protein Sequence |
>Acyl-CoA wax alcohol acyltransferase 1
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPE
RGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEA
TGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVG
GVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKF
QSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHA
LYMDALHKLFDQHKTHYGCSETQKLFFL
|
| Enzyme 2 Number of Residues |
328 |
| Enzyme 2 Molecular Weight |
37758.8 |
| Enzyme 2 Theoretical pI |
9.02 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 2 Specific Function |
Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20) |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
123227401  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q58HT5  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AWAT1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>987 bp
ATGGCTCATTCCAAGCAGCCTAGTCACTTCCAGAGTCTGATGCTTCTGCAGTGGCCTTTG
AGCTACCTTGCCATCTTTTGGATCTTGCAGCCATTGTTCGTCTACCTGCTGTTTACATCC
TTGTGGCCGCTACCAGTGCTTTACTTTGCCTGGTTGTTCCTGGACTGGAAGACCCCAGAG
CGAGGTGGCAGGCGTTCGGCCTGGGTAAGGAACTGGTGTGTCTGGACCCACATCAGGGAC
TATTTCCCCATTACGATCCTGAAGACAAAGGACCTATCACCTGAGCACAACTACCTCATG
GGGGTTCACCCCCATGGCCTCCTGACCTTTGGCGCCTTCTGCAACTTCTGCACTGAGGCC
ACAGGCTTCTCGAAGACCTTCCCAGGCATCACTCCTCACTTGGCCACGCTGTCCTGGTTC
TTCAAGATCCCCTTTGTTAGGGAGTACCTCATGGCCAAAGGTGTGTGCTCTGTGAGCCAG
CCAGCCATCAACTATCTGCTGAGCCATGGCACTGGCAACCTCGTGGGCATTGTAGTGGGA
GGTGTGGGTGAGGCCCTGCAAAGTGTGCCCAACACCACCACCCTCATCCTCCAGAAGCGC
AAGGGGTTCGTGCGCACAGCCCTCCAGCATGGGGCTCATCTGGTCCCCACCTTCACTTTT
GGGGAAACTGAGGTGTATGATCAGGTGCTGTTCCATAAGGATAGCAGGATGTACAAGTTC
CAGAGCTGCTTCCGCCGTATCTTTGGTTTCTACTGTTGTGTCTTCTATGGACAAAGCTTC
TGTCAAGGCTCCACTGGGCTCCTGCCATACTCCAGGCCTATTGTCACTGTGGTTGGGGAG
CCTCTGCCACTGCCCCAAATTGAAAAGCCAAGCCAGGAGATGGTGGACAAATACCATGCA
CTTTATATGGATGCTCTGCACAAACTGTTCGACCAGCATAAGACCCACTATGGCTGCTCA
GAGACCCAAAAGCTGTTTTTCCTGTGA
|
| Enzyme 2 GenBank Gene ID |
AL357752  |
| Enzyme 2 GeneCard ID |
AWAT1  |
| Enzyme 2 GenAtlas ID |
AWAT1  |
| Enzyme 2 HGNC ID |
HGNC:23252  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- 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
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
12898 |
| Enzyme 3 Name |
Acyl-CoA wax alcohol acyltransferase 2 |
| Enzyme 3 Synonyms |
- Diacylglycerol O-acyltransferase 2-like protein 4
- Diacylglycerol O-acyltransferase candidate 4
- hDC4
- Long-chain-alcohol O-fatty-acyltransferase 2
- Multifunctional O-acyltransferase
- Wax synthase
- hWS
|
| Enzyme 3 Gene Name |
AWAT2 |
| Enzyme 3 Protein Sequence |
>Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
|
| Enzyme 3 Number of Residues |
333 |
| Enzyme 3 Molecular Weight |
38093.2 |
| Enzyme 3 Theoretical pI |
9.69 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 3 Specific Function |
Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
49854214  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q6E213  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
AWAT2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1002 bp
ATGCTCTTGCCCTCTAAGAAGGACCTCAAGACTGCCCTGGATGTCTTTGCTGTTTTCCAG
TGGTCCTTCAGTGCCTTGCTTATCACAACCACTGTGATTGCTGTCAACCTCTACCTGGTG
GTGTTCACACCATACTGGCCTGTCACTGTGCTTATTCTTACCTGGCTGGCTTTTGACTGG
AAGACCCCTCAGCGAGGCGGCCGCCGGTTTACCTGTGTGAGGCACTGGCGCCTGTGGAAA
CACTACAGCGATTATTTCCCTCTCAAGCTTCTGAAGACTCATGACATCTGCCCCAGCCGC
AACTACATCCTCGTCTGCCACCCTCATGGGCTCTTTGCCCATGGATGGTTTGGCCACTTT
GCCACAGAGGCCTCAGGCTTCTCCAAGATATTTCCTGGCATCACCCCTTACATACTCACA
CTGGGAGCCTTTTTCTGGATGCCTTTCCTCAGAGAATATGTAATGTCTACAGGGGCCTGC
TCTGTGAGTCGATCCTCCATTGACTTTCTGCTGACTCATAAAGGCACAGGCAACATGGTC
ATTGTGGTGATTGGTGGACTGGCTGAGTGCAGATACAGCCTGCCAGGTTCTTCTACCCTG
GTGTTGAAGAACCGGTCTGGCTTTGTGCGCATGGCCCTTCAGCATGGGGTGCCTCTAATA
CCTGCCTATGCCTTTGGGGAGACGGACCTCTATGATCAGCACATTTTCACTCCTGGTGGC
TTTGTCAACCGCTTCCAGAAGTGGTTCCAGAGCATGGTACACATCTACCCTTGTGCTTTC
TATGGACGTGGCTTCACCAAGAACTCCTGGGGCCTTCTGCCCTATAGTCGGCCTGTAACC
ACCATCGTCGGGGAGCCTCTACCAATGCCCAAGATTGAGAATCCAAGCCAGGAGATCGTG
GCTAAATATCACACACTCTATATTGATGCCCTACGTAAACTGTTTGACCAGCATAAGACC
AAGTTTGGTATCTCAGAGACCCAGGAGCTGGAGATAATTTGA
|
| Enzyme 3 GenBank Gene ID |
AY605053  |
| Enzyme 3 GeneCard ID |
AWAT2  |
| Enzyme 3 GenAtlas ID |
AWAT2  |
| Enzyme 3 HGNC ID |
HGNC:23251  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Cheng JB, Russell DW: Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. J Biol Chem. 2004 Sep 3;279(36):37798-807. Epub 2004 Jun 27. [PubMed
]
- 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
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
- Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed
]
- Yen CL, Brown CH 4th, Monetti M, Farese RV Jr: A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J Lipid Res. 2005 Nov;46(11):2388-97. Epub 2005 Aug 16. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
15268 |
| Enzyme 4 Name |
cDNA FLJ75813, highly similar to Homo sapiens lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase) (LRAT), mRNA (Lecithin retinol acyltransferase) (Phosphatidylcholine-- retinol O-acyltransferase) |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
LRAT |
| Enzyme 4 Protein Sequence |
>cDNA FLJ75813, highly similar to Homo sapiens lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase) (LRAT), mRNA (Lecithin retinol acyltransferase) (Phosphatidylcholine-- retinol O-acyltransferase)
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
|
| Enzyme 4 Number of Residues |
230 |
| Enzyme 4 Molecular Weight |
25703 |
| Enzyme 4 Theoretical pI |
7.54 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158258633  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8K983  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8K983_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>693 bp
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCGAAGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGTACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
|
| Enzyme 4 GenBank Gene ID |
AK292598  |
| Enzyme 4 GeneCard ID |
A8K983  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |