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Literature summary for 1.3.1.44 extracted from

  • Prasad, M.R.; Nagi, M.N.; Cook, L.; Cinti, D.L.
    Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase (1983), Biochem. Biophys. Res. Commun., 113, 659-665.
    View publication on PubMed
Search for more literature for 1.3.1.44

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Rattus norvegicus
-
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.005
-
 substrate trans-2-octenoyl-CoA with NADH Rattus norvegicus
0.02
-
 substrate trans-2-hexadecenoyl-CoA with NADH Rattus norvegicus
0.027
-
 substrate trans-2-hexadecenoyl-CoA with NADPH Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information long-chain substrates preferred Rattus norvegicus ?
-
 ?
trans-2-hexadecenoyl-CoA + NADH
-
 Rattus norvegicus hexadecanoyl-CoA + NAD+
-
 ?
trans-2-octenoyl-CoA + NADH
-
 Rattus norvegicus octanoyl-CoA + NAD+
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADH preferred cofactor with substrates of higher chain length Rattus norvegicus
NADPH
-
 Rattus norvegicus