EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.50 | a long-chain acyl-CoA + NADPH + H+ |
- |
Cryptosporidium parvum |
a long-chain aldehyde + CoA + NADP+ |
- |
? |
1.2.1.50 | arachidoyl-CoA + NADP+ |
29% of the activity with NADPH |
Acinetobacter sp. |
eicosanal + CoA + NADPH |
- |
? |
1.2.1.50 | arachidoyl-CoA + NADP+ |
29% of the activity with NADPH |
Acinetobacter sp. M-1 |
eicosanal + CoA + NADPH |
- |
? |
1.2.1.50 | hexadecanoyl-CoA + NADPH + H+ |
- |
Pisum sativum |
hexadecanal + CoA + NADP+ |
- |
? |
1.2.1.50 | lauroyl-CoA + NADP+ |
33% of the activity with myristoyl-CoA |
Acinetobacter sp. |
dodecanal + CoA + NADPH |
- |
? |
1.2.1.50 | lauroyl-CoA + NADP+ |
33% of the activity with myristoyl-CoA |
Acinetobacter sp. M-1 |
dodecanal + CoA + NADPH |
- |
? |
1.2.1.50 | more |
substrates with carbon chain lengths shorter thah 8 do not show any activity |
Acinetobacter sp. |
? |
- |
? |
1.2.1.50 | more |
catalyses the formation of a fatty alcohol from an acyl-CoA |
Arabidopsis thaliana |
? |
- |
? |
1.2.1.50 | more |
enzyme only utilizes very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16, enzyme is capable of using NADPH and NADH as electron donors, but prefers NADPH to NADH |
Cryptosporidium parvum |
? |
- |
? |
1.2.1.50 | more |
in contrast to other prokaryotes, the enzyme performs the two reduction steps from acyl-CoA to fatty alcohol in a single step which is typical for eukaryotes |
Marinobacter nauticus |
? |
- |
? |