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

BRENDA support

Literature summary for 1.3.1.10 extracted from

  • Saito, K.; Kawaguchi, A.; Seyama, Y.; Yamakawa, T.; Okuda, S.
    Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli (1981), Eur. J. Biochem., 116, 581-586.
    View publication on PubMed
Search for more literature for 1.3.1.10

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
which also catalyzes the reduction of enoyl-CoA substrates Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acyl-[acyl-carrier protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ syn addition via 2Re,3Si attack on double bond Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-decenoyl-[acyl-carrier protein] + NADPH syn addition of hydrogen via a 2-Re,3-Si attack on the double bond Escherichia coli decanoyl-[acyl-carrier protein] + NADP+
-
 ?
additional information inactive with enoyl-CoA substrates Escherichia coli ?
-
 ?
additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Escherichia coli ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADPH stereospecificity of NADPH is pro-4S Escherichia coli