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Literature summary for 1.2.1.42 extracted from

  • Vioque, J.; Kolattukudy, P.E.
    Resolution and purification of an aldehyde-generating and an alcohol-generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.) (1997), Arch. Biochem. Biophys., 340, 64-72.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
NADH aldehyde generation Pisum sativum
0.0032
-
NADPH aldehyde generation Pisum sativum
0.0075
-
NADPH alcohol generation Pisum sativum
0.0151
-
NADH alcohol generation Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
x * 28000, aldehyde-generating enzyme, SDS-PAGE Pisum sativum
58000
-
x * 58000, alcohol-generating enzyme, SDS-PAGE Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
alcohol-generating and aldehyde-generating acyl-CoA reductases, Blue A agarose, gel filtration, hexadecanoyl-CoA affinity chromatography Pisum sativum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0024
-
alcohol-generating enzyme Pisum sativum
0.96
-
aldehyde-generating enzyme Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hexadecanoyl-CoA + NAD(P)H
-
Pisum sativum hexadecanal + NAD(P)+
-
?
hexadecanoyl-CoA + NADH + H+
-
Pisum sativum hexadecanal + CoA + NAD+
-
r

Subunits

Subunits Comment Organism
? x * 58000, alcohol-generating enzyme, SDS-PAGE Pisum sativum
? x * 28000, aldehyde-generating enzyme, SDS-PAGE Pisum sativum

Cofactor

Cofactor Comment Organism Structure
NAD(P)H NADPH is prefered for alcohol formation, NADH is prefered for aldehyde formation Pisum sativum