EC Number |
Cofactor |
Reference |
---|
1.5.1.36 | NADH |
although the HpaC enzyme can also use NADPH as a substrate, its specific activities on FMN, FAD, and riboflavin are more than 2 orders of magnitude lower than those observed in the presence of NADH |
438899 |
1.5.1.36 | NADH |
HpaC, the small component of the 4-hydroxyphenylacetate 3-monooxygenase, is recombinantly overproduced in Escherichia coli K12 and catalyzes the reduction of free flavins by NADH in preference to NADPH |
438899 |
1.5.1.36 | NADPH |
although the HpaC enzyme can also use NADPH as a substrate, its specific activities on FMN, FAD, and riboflavin are more than 2 orders of magnitude lower than those observed in the presence of NADH |
438899 |
1.5.1.36 | FADH2 |
- |
658006 |
1.5.1.36 | NADH |
- |
658006, 711238, 720976, 726414, 741680, 741794, 743224, 743241, 743891, 744377, 764038, 765735 |
1.5.1.36 | NADPH |
- |
658006, 720976 |
1.5.1.36 | FAD |
- |
712723, 741680 |
1.5.1.36 | NADH |
no activity with NADPH |
712723 |
1.5.1.36 | NADH |
the enzyme prefers NADH as a substrate |
724294 |
1.5.1.36 | FMN |
each subunit binds one FMN as cofactor |
726414 |