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Results 1 - 10 of 21 > >>
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
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
precorrin-3B + NAD+ + H2O
-
?
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
precorrin-3B + NAD+ + H2O
-
?
more
biosynthesis of vitamin B12
?
-
?
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
?
-
-
precorrin-3 + NADH + H+ + O2
-
precorrin-3x + NAD+ + H2O
-
ir
precorrin-3 + NADH + H+ + O2
biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
precorrin-3x + NAD+ + H2O
-
ir
precorrin-3A + NADH + H+ + O2
-
precorrin-3B + NAD+ + H2O
-
?
precorrin-3A + NADH + H+ + O2
-
precorrin-3B + NAD+ + H2O
-
ir
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
precorrin-3B + NAD+ + H2O
-
ir
precorrin-3A + NADH + H+ + O2
first step in the aerobic pathway of viamin B12 biosynthesis
precorrin-3B + NAD+ + H2O
-
?
Results 1 - 10 of 21 > >>