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IUBMB CommentsAn iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.
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precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
additional information
?
-
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
-
-
-
ir
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
-
-
-
ir
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
-
biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
-
-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
-
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
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
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
first step in the aerobic pathway of viamin B12 biosynthesis
-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
the Pseudomonas denitrificans enzyme is active in vivo but inactive 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), the mononuclear non-heme iron is not reducible and probably rapidly inactivated outside the bacterium
-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
-
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
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
-
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
-
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
biosynthesis of vitamin B12
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
-
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
biosynthesis of vitamin B12
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
-
-
?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
-
-
?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
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
-
?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
the enzyme generates a hydroxy lactone intermediate
-
?
additional information
?
-
-
biosynthesis of vitamin B12
-
?
additional information
?
-
-
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
-
?
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precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
-
biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
additional information
?
-
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
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
-
ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
first step in the aerobic pathway of viamin B12 biosynthesis
-
-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
the Pseudomonas denitrificans enzyme is active in vivo but inactive 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), the mononuclear non-heme iron is not reducible and probably rapidly inactivated outside the bacterium
-
-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
-
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
-
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
biosynthesis of vitamin B12
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
-
biosynthesis of vitamin B12
aerobic incubation with CobG alone, if CobJ and S-adenosyl-L-methionine are included the product is precorrin-4
ir
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
-
-
-
?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
-
-
-
?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
-
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
-
-
?
additional information
?
-
-
biosynthesis of vitamin B12
-
?
additional information
?
-
-
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
-
-
?
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C358A
no activity, no Fe-S center
C364A
no activity, no Fe-S center
C394A
no activity, no Fe-S center
C398A
no activity, no Fe-S center
C42A
active, Fe-S center present
H390A
active, Fe-S center present
C358A
-
no activity, no Fe-S center
C364A
-
no activity, no Fe-S center
C394A
-
no activity, no Fe-S center
C42A
-
active, Fe-S center present
C358A
-
no activity, no Fe-S center
C364A
-
no activity, no Fe-S center
C394A
-
no activity, no Fe-S center
C398A
-
no activity, no Fe-S center
C42A
-
active, Fe-S center present
H390A
-
active, Fe-S center present
additional information
for in vivo enzyme assays an Escherichia coli strain with all necessary genes for the production of cobyric acid except the cobG gene is used for complementation studies in combination with wild-type and mutant cobG genes (site-directed mutagenesis), for in vitro assays an Escherichia coli strain with a coupled multi-enzyme system (plasmid for the production of hydrogenobyrinic acid lacking the cobG gene) is combined with crude extract of an Escherichia coli strain overproducing GobG
additional information
-
for in vivo enzyme assays an Escherichia coli strain with all necessary genes for the production of cobyric acid except the cobG gene is used for complementation studies in combination with wild-type and mutant cobG genes (site-directed mutagenesis), for in vitro assays an Escherichia coli strain with a coupled multi-enzyme system (plasmid for the production of hydrogenobyrinic acid lacking the cobG gene) is combined with crude extract of an Escherichia coli strain overproducing GobG
additional information
-
for in vivo enzyme assays an Escherichia coli strain with all necessary genes for the production of cobyric acid except the cobG gene is used for complementation studies in combination with wild-type and mutant cobG genes (site-directed mutagenesis), for in vitro assays an Escherichia coli strain with a coupled multi-enzyme system (plasmid for the production of hydrogenobyrinic acid lacking the cobG gene) is combined with crude extract of an Escherichia coli strain overproducing GobG
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centrifugation of cells, pellet resuspended in binding buffer (20 mM Tris-HCl, pH 8.0, containing 0.5 M NaCl and 5 mM imidazole), cells broken up with a cell disrupter or sonicated, centrifugation, supernatant transferred to an anaerobic glove box, applied to a metal affinity chromatography column charged with Ni2+, washed with buffer with 20 mM imidazole, elution with 400 mM imidazole
centrifugation of cells, pellet resuspended in binding buffer (20 mM Tris-HCl, pH 8.0, containing 0.5 M NaCl and 5 mM imidazole), cells broken up with a cell disrupter or sonicated, centrifugation, supernatant transferred to an anaerobic glove box, applied to a metal affinity chromatography column charged with Ni2+, washed with buffer with 20 mM imidazole, elution with 400 mM imidazole
-
centrifugation of cells, pellet resuspended in binding buffer (20 mM Tris-HCl, pH 8.0, containing 0.5 M NaCl and 5 mM imidazole), cells broken up with a cell disrupter or sonicated, centrifugation, supernatant transferred to an anaerobic glove box, applied to a metal affinity chromatography column charged with Ni2+, washed with buffer with 20 mM imidazole, elution with 400 mM imidazole
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Roessner, C.A.; Spencer, J.B.; Ozaki, S.; Min, C.; Atshaves, B.P.; Nayar, P.; Anousis, N.; Stolowich, N.J.; Holderman, M.T.; Scott, A.I.
Overexpression in Escherichia coli of 12 vitamin B12 biosynthetic enzymes
Protein Expr. Purif.
6
155-163
1995
Pseudomonas denitrificans (nomen rejiciendum)
brenda
Scott, A.I.; Roessner, C.A.; Stolowich, N.J.; Spencer, J.B.; Min, C.; Ozaki, S.I.
Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative ring contraction and insertion of the fourth methyl group
FEBS Lett.
331
105-108
1993
Pseudomonas denitrificans (nomen rejiciendum)
brenda
Debussche, L.; Thibaut, D.; Cameron, B.; Crouzet, J.; Blanche, F.
Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans
J. Bacteriol.
175
7430-7440
1993
Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas denitrificans (nomen rejiciendum) SC510 (RifT)
brenda
Stamford, N.P.; Duggan, S.; Li, Y.; Alanine, A.I.; Crouzet, J.; Battersby, A.R.
Biosynthesis of vitamin B12: the multi-enzyme synthesis of precorrin-4 and factor IV
Chem. Biol.
4
445-451
1997
Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas denitrificans (nomen rejiciendum) G3575
brenda
Heldt, D.; Lawrence, A.D.; Lindenmeyer, M.; Deery, E.; Heathcote, P.; Rigby, S.E.; Warren, M.J.
Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation
Biochem. Soc. Trans.
33
815-819
2005
Rhodobacter capsulatus
brenda
Iida, K.; Ohtaka, K.; Kajiwara, M.
Mechanism of the ring contraction process in vitamin B12 biosynthesis by the anaerobe Propionibacterium shermanii under aerobic conditions
FEBS J.
274
3475-3481
2007
Pseudomonas denitrificans (nomen rejiciendum)
brenda
Schroeder, S.; Lawrence, A.D.; Biedendieck, R.; Rose, R.S.; Deery, E.; Graham, R.M.; McLean, K.J.; Munro, A.W.; Rigby, S.E.; Warren, M.J.
Demonstration that CobG, the monooxygenase associated with the ring contraction process of the aerobic cobalamin (vitamin B12) biosynthetic pathway, contains an Fe-S center and a mononuclear non-heme iron center
J. Biol. Chem.
284
4796-4805
2009
Pseudomonas denitrificans (nomen rejiciendum), Brucella melitensis (Q8YHT1), Brucella melitensis 16M (Q8YHT1)
brenda
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1.14.13.83 precorrin-3B synthase
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