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Literature summary for 1.2.1.42 extracted from

  • Johnson, R.C.; Gilbertson, J.R.
    Isolation, characterization, and partial purification of a fatty acyl coenzyme A reductase from bovine cardiac muscle (1972), J. Biol. Chem., 247, 6991-6998.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
HgCl2
-
Bos taurus
p-chloromercuribenzoate
-
Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85000 95000 gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
heating, ammonium sulfate, gel filtration Bos taurus

Reaction

Reaction Comment Organism Reaction ID
hexadecanal + CoA + NAD+ = hexadecanoyl-CoA + NADH + H+ also acts, more slowly, on octadecanoyl-CoA Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
cardiac muscle
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
321
-
-
Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hexadecanoyl-CoA + NADH reduction of NAD+ is at most 5% of the rate of NADH oxidoreduction, the enzyme is primarily a reductase and not an aldehyde dehydrogenase Bos taurus hexadecanal + NAD+ + CoA
-
?
octadecanoyl-CoA + NADH slowly, octadecanoyl-CoA is identical with stearoyl-CoA Bos taurus octadecanal + NAD+ + CoA
-
?

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 pH 6.5 and pH 9.0: about 20% of maximum activity Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Bos taurus