Sequence of AK1A1_RAT
EC Number:1.1.1.33
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R)-mevalonate + NADP+ = mevaldate + NADPH + H+
Other sequences found for EC No. 1.1.1.33
General information:
Sequence
0 MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY GNETEIGEAL
60 KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA DLQLEYLDLY LMHWPYAFER
120 GDNPFPKNAD GTVKYDSTHY KETWKALEAL VAKGLVKALG LSNFSSRQID DVLSVASVRP
180 AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK
240 HGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV
300 PMITVDGKRV PRDAGHPLYP FNDPY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
512834
Takahashi M.,Fujii J.,Teshima T.,Suzuki K.,Shiba T.,Taniguchi N.
Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression.
Gene
127
249-253
1993
512835
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
512836
Takahashi M.,Lu Y.B.,Myint T.,Fujii J.,Wada Y.,Taniguchi N.
In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites.
Biochemistry
34
1433-1438
1995
512838
Beedle A.S.,Rees H.H.,Goodwin T.W.
Some properties and a suggested reclassification of mevaldate reductase.
Biochem. J.
139
205-209
1974
512840
Takahashi M.,Miyata S.,Fujii J.,Inai Y.,Ueyama S.,Araki M.,Soga T.,Fujinawa R.,Nishitani C.,Ariki S.,Shimizu T.,Abe T.,Ihara Y.,Nishikimi M.,Kozutsumi Y.,Taniguchi N.,Kuroki Y.
In vivo role of aldehyde reductase.
Biochim. Biophys. Acta
1820
1787-1796
2012
512841
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
512842
Kurahashi T.,Kwon M.,Homma T.,Saito Y.,Lee J.,Takahashi M.,Yamada K.,Miyata S.,Fujii J.
Reductive detoxification of acrolein as a potential role for aldehyde reductase (AKR1A) in mammals.
Biochem. Biophys. Res. Commun.
452
136-141
2014
