EC Number |
Cofactor |
Reference |
---|
1.1.1.422 | more |
no activity with NADP+ |
755862 |
1.1.1.422 | NAD+ |
- |
752351, 755862 |
1.1.1.422 | NAD+ |
no apparent activity with NADP(H)+ and full catalytic activity with NAD(H). The preference for NADH makes the utilization of the enzyme an attractive for industrial applications, since NADH is more stable and less expensive than NADPH under operational reaction conditions |
752351 |
1.1.1.422 | NAD+ |
the enzyme displays no apparent activity with NADP(H) and full catalytic activity with NAD(H). A model of the active site in complex with NAD+ and 1-phenyl-1,2-propanedione suggests key roles for S143 and W152 in recognition of the substrate and positioning for the reduction reaction |
752351 |
1.1.1.422 | NAD+ |
the enzyme is strictly NAD+-dependent |
755862 |
1.1.1.422 | NADH |
- |
752351 |
1.1.1.422 | NADH |
no apparent activity with NADP(H)+ and full catalytic activity with NAD(H). The preference for NADH makes the utilization of the enzyme an attractive for industrial applications, since NADH is more stable and less expensive than NADPH under operational reaction conditions |
752351 |
1.1.1.422 | NADH |
the enzyme displays no apparent activity with NADP(H) and full catalytic activity with NAD(H) |
752351 |