Sequence of ADHX_HUMAN
EC Number:1.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 1.1.1
EC Number:1.1.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Other sequences found for EC No. 1.1.1.1
EC Number:1.1.1.284
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.284
EC Number:1.2.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 1.2.1.1
General information:
Sequence
0 MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGC
60 FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
120 GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPLAPLDKVC LLGCGISTGY
180 GAAVNTAKLE PGSVCAVFGL GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC
240 INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE
300 IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL SFDEINKAFE
360 LMHSGKSIRT VVKI
Download this sequence
in fasta formatDownload all sequences for 1.2.1.1
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
387216
Sharma C.P.,Fox E.A.,Holmquist B.,Joernvall H.,Vallee B.L.
cDNA sequence of human class III alcohol dehydrogenase.
Biochem. Biophys. Res. Commun.
164
631-637
1989
387217
Giri P.R.,Krug J.F.,Kozak C.,Moretti T.,O'Brien S.J.,Seuanez H.N.,Goldman D.
Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA.
Biochem. Biophys. Res. Commun.
164
453-460
1989
387218
Hur M.W.,Edenberg H.J.
Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase.
Gene
121
305-311
1992
387222
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
387223
Kaiser R.,Holmquist B.,Hempel J.,Vallee B.L.,Joernvall H.
Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes.
Biochemistry
27
1132-1140
1988
387224
Holmquist B.,Moulis J.-M.,Engeland K.,Vallee B.L.
Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase.
Biochemistry
32
5139-5144
1993
387225
Engeland K.,Hoeoeg J.-O.,Holmquist B.,Estonius M.,Joernvall H.,Vallee B.L.
Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation.
Proc. Natl. Acad. Sci. U.S.A.
90
2491-2494
1993
387226
Collins X.H.,Harmon S.D.,Kaduce T.L.,Berst K.B.,Fang X.,Moore S.A.,Raju T.V.,Falck J.R.,Weintraub N.L.,Duester G.,Plapp B.V.,Spector A.A.
Omega-oxidation of 20-hydroxyeicosatetraenoic acid (20-HETE) in cerebral microvascular smooth muscle and endothelium by alcohol dehydrogenase 4.
J. Biol. Chem.
280
33157-33164
2005
387227
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
387228
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
387229
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
387230
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
387231
Yang Z.-N.,Bosron W.F.,Hurley T.D.
Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase.
J. Mol. Biol.
265
330-343
1997
