Sequence of BDH_BOVIN
EC Number:1.1.1.30
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
Other sequences found for EC No. 1.1.1.30
General information:
Sequence
0 MLTARLSRPL SQLPRKTLNF SDRENGTRGS LLLYSAPFVP VGRRTYAASV DPVGSKAVLI
60 TGCDSGFGFS LAKHLHSEGF LVFAGCLMKD KGSDGVKELD SMKSDRLRTV QLNVCKSEEV
120 DKAAEVIRSS LEDPEKGLWG LVNNAGISTF GDVEFTSMET YKEVAEVNLW GTVRVTKAFL
180 PLIRRAKGRV VNISSMMGRM ANVARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN
240 FIAATSLYGG TERIQAIANK MWEELPEVVR QDYGRKYFDE KVARMESYCT SGSTDTSPVI
300 KAVTHALTAT TPYTRYHPMD YYWWLRMQIM THFPGAISDR IYIH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1162268
Marks A.R.,McIntyre J.O.,Duncan T.M.,Erdjument-Bromage H.,Tempst P.,Fleischer S.
Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart.
J. Biol. Chem.
267
15459-15463
1992
1162269
Prasad P.V.,Hatefi Y.
Amino acid sequences of two tryptic peptides from D(-)-beta-hydroxybutyrate dehydrogenase radiolabeled at essential carboxyl and sulfhydryl groups.
Biochem. Int.
12
941-949
1986
1162270
McIntyre J.O.,Bock H.G.,Fleischer S.
The orientation of D-beta-hydroxybutyrate dehydrogenase in the mitochondrial inner membrane.
Biochim. Biophys. Acta
513
255-267
1978
1162271
McIntyre J.O.,Churchill P.,Maurer A.,Berenski C.J.,Jung C.Y.,Fleischer S.
Target size of D-beta-hydroxybutyrate dehydrogenase. Functional and structural molecular weight based on radiation inactivation.
J. Biol. Chem.
258
953-959
1983
1162272
Rudy B.,Dubois H.,Mink R.,Trommer W.E.,McIntyre J.O.,Fleischer S.
Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme: lecithin acts as an allosteric modulator to enhance the affinity for coenzyme.
Biochemistry
28
5354-5366
1989
