Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.8 extracted from

  • Maitra, S.K.; Kumar, S.
    Crotonyl coenzyme A reductase activity of bovine mammary fatty acid synthetase (1974), J. Biol. Chem., 249, 111-117.
    View publication on PubMed
Search for more literature for 1.3.1.8

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol enhancement in the range of 5-10 mM Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
dithiothreitol above 10 mM Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0033
-
 trans-crotonyl-CoA
-
 Bos taurus
0.0067
-
 butyryl-CoA
-
 Bos taurus
0.13
-
 acetyl-CoA
-
 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
fatty acid synthetase, also exhibiting crotonyl-CoA reductase activity Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
mammary gland
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + NADPH + H+
-
 Bos taurus ?
-
 r
crotonyl-CoA + NAD(P)H
-
 Bos taurus butanoyl-CoA + NADP+
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Bos taurus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 42
-
 Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 8.5
-
 Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH 20fold higher concentration of NADH compared to NADPH results in 50% of NADPH activity Bos taurus
NADPH
-
 Bos taurus