EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
biosynthesis of vitamin B12 |
Pseudomonas denitrificans (nom. rej.) G3575 |
precorrin-3B + NAD+ + H2O |
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4 |
ir |
1.14.13.83 | precorrin-3 + NADH + H+ + O2 |
biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction |
Pseudomonas denitrificans (nom. rej.) |
precorrin-3x + NAD+ + H2O |
- |
ir |
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
first step in the aerobic pathway of viamin B12 biosynthesis |
Pseudomonas denitrificans (nom. rej.) |
precorrin-3B + NAD+ + H2O |
- |
? |
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
pathway to coenzyme B12, biosynthesis of the corrin macrocycle, catalyzes a complex oxidative reaction involving C20 hydroxylation and gamma-lactone formation from ring-A acetate to C1 |
Pseudomonas denitrificans (nom. rej.) |
precorrin-3B + NAD+ + H2O |
- |
ir |
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
pathway to coenzyme B12, biosynthesis of the corrin macrocycle, catalyzes a complex oxidative reaction involving C20 hydroxylation and gamma-lactone formation from ring-A acetate to C1 |
Pseudomonas denitrificans (nom. rej.) SC510 (RifT) |
precorrin-3B + NAD+ + H2O |
- |
ir |
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
the Brucella melitensis enzyme is fully active in vitro (20 mM Tris-HCl buffer, pH 8.0, with 100 mM NaCl, S-adenosyl-L-methionine (SAM), 5-aminolevulinic acid (ALA) and NADPH, aerobic, dark, 4°C) and the mononuclear non-heme iron is reducible by dithionite and then is able to react with NO as oxygen analogue in the presence of the substrate |
Brucella melitensis |
precorrin-3B + NAD+ + H2O |
- |
? |
1.14.13.83 | precorrin-3A + NADH + H+ + O2 |
the Brucella melitensis enzyme is fully active in vitro (20 mM Tris-HCl buffer, pH 8.0, with 100 mM NaCl, S-adenosyl-L-methionine (SAM), 5-aminolevulinic acid (ALA) and NADPH, aerobic, dark, 4°C) and the mononuclear non-heme iron is reducible by dithionite and then is able to react with NO as oxygen analogue in the presence of the substrate |
Brucella melitensis 16M |
precorrin-3B + NAD+ + H2O |
- |
? |
1.14.13.83 | precorrin-3A + NADH + O2 |
the enzyme generates a hydroxy lactone intermediate |
Rhodobacter capsulatus |
precorrin-3B + NAD+ + H2O |
- |
? |
1.14.13.83 | precorrin-3A + NADH + O2 |
the enzyme is involved in ring contraction, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed, and cobalt chelation during aerobic synthesis of vitamin B12, the catalytic cycle of CobZ, overview |
Rhodobacter capsulatus |
precorrin-3B + NAD+ + H2O |
- |
? |
1.14.13.83 | more |
the enzyme is involved in the mechanism of the ring contraction process during vitamin B12 biosynthesis, comparison to the ring contraction process reaction pathway under anaerobic conditions in Propionibacterium freudenreichii ssp. shermanii, overview |
Pseudomonas denitrificans (nom. rej.) |
? |
- |
? |