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Literature summary for 1.1.1.30 extracted from

  • Klein, K.; Rudy, B.; McIntyre, J.O.; Fleischer, S.; Trommer, W.E.
    Specific interaction of(R)-3-hydroxybutyrate dehydrogenase with membrane phosphatidylcholine as studied by ESR spectroscopy in oriented phospholipid multilayers: coenzyme binding enhances the interaction with phosphatidylcholine (1996), Biochemistry, 35, 3044-3049.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylcholine required for formation of tight and functional complexes of enzyme with NAD+, coenzyme binding strengthens the interaction of the enzyme with phosphatidylcholine Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Bos taurus 5737
-
mitochondrion
-
Bos taurus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-3-hydroxybutanoate + NAD+ Bos taurus
-
acetoacetate + NADH
-
r

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-3-hydroxybutanoate + NAD+
-
Bos taurus acetoacetate + NADH
-
r

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bos taurus