EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.3.1.86 | (E)-but-2-enoyl-CoA + NADPH + H+ |
- |
Streptomyces virginiae |
butanoyl-CoA + NADP+ |
- |
? |
1.3.1.86 | crotonyl-CoA + NADH + ferredoxin |
- |
Clostridioides difficile |
butyryl-CoA + ? |
- |
? |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
- |
Streptomyces virginiae |
butyryl-CoA + NADP+ |
- |
? |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
- |
Streptomyces virginiae |
butyryl-CoA + NADP+ |
- |
ir |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
- |
Streptomyces collinus |
butyryl-CoA + NADP+ |
- |
? |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
- |
Streptomyces hygroscopicus subsp. ascomyceticus |
butyryl-CoA + NADP+ |
- |
? |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
the overall reduction of crotonyl-CoA proceeds in an anti fashion, the reaction proceeds with transfer of the hydrogen from the pro-4S position of NADPH to the Re face of the beta-carbon of crotonyl-CoA |
Streptomyces collinus |
butyryl-CoA + NADP+ |
- |
? |
1.3.1.86 | crotonyl-CoA + NADPH + H+ |
the enzyme exhibits a high substrate specificity for crotonyl-CoA |
Streptomyces collinus |
butanoyl-CoA + NADP+ |
- |
? |
1.3.1.86 | more |
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax |
Bos taurus |
? |
- |
? |
1.3.1.86 | more |
the enzyme is unable to catalyze the reduction of any other enoyl-CoA thioesters (acryloyl-CoA, trans-2-pentenoyl-CoA, trans-hexenoyl-CoA, trans-2-octenoyl-CoA, trans-2-dodecenoyl-CoA, trans-2-hexadecenoyl-CoA) or to utilize NADH as an electron donor. The enzyme is unable to reduce either the N-acetylcysteamine or the pantetheine thioester of crotonic acid |
Streptomyces collinus |
? |
- |
? |