EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.5.1.15 | 5,10-methenyltetrahydrofolate + NADH + H+ |
- |
Mycolicibacterium smegmatis |
5,10-methylenetetrahydrofolate + NAD+ |
- |
ir |
1.5.1.15 | 5,10-methenyltetrahydrofolate + NADH + H+ |
- |
Mycolicibacterium smegmatis ATCC 700084 |
5,10-methylenetetrahydrofolate + NAD+ |
- |
ir |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
- |
Mus musculus |
5,10-methenyltetrahydrofolate + NADH |
- |
? |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
- |
Homo sapiens |
5,10-methenyltetrahydrofolate + NADH |
- |
? |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
enzyme provides one-carbon units for purine synthesis during embryogenesis, metabolism overview |
Mus musculus |
5,10-methenyltetrahydrofolate + NADH |
- |
? |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
N-terminal catalytic domain |
Mus musculus |
5,10-methenyltetrahydrofolate + NADH |
- |
? |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
- |
Escherichia coli |
5,10-methenyltetrahydrofolate + NADH + H+ |
- |
r |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
- |
Mus musculus |
5,10-methenyltetrahydrofolate + NADH + H+ |
- |
r |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420 |
Methanosarcina barkeri |
5,10-methenyltetrahydrofolate + NADH + H+ |
- |
? |
1.5.1.15 | 5,10-methylenetetrahydrofolate + NAD+ |
enzyme binding structure analysis, overview |
Escherichia coli |
5,10-methenyltetrahydrofolate + NADH + H+ |
- |
r |