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Information on EC 1.14.13.83 - precorrin-3B synthase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.83
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RECOMMENDED NAME
GeneOntology No.
precorrin-3B synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O
An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosynthesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. This enzyme carries out the first of the four steps, yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ), C-11 (CobM) and C-1 (CobF
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precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O
reaction mechanism of CobZ
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating)
An 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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CAS REGISTRY NUMBER
COMMENTARY
152787-63-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in bacteria such as Rhodobacter capsulatus CobG is substituted by an isofunctional protein called CobZ
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
vitamin B12/cobalamin biosynthesis, the 4Fe-4S center, mononuclear non-heme iron, is necessary for enzyme activity
metabolism
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vitamin B12/cobalamin biosynthesis, the 4Fe-4S center, mononuclear non-heme iron, is necessary for enzyme activity
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
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-
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ir
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
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-
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ir
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
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biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
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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
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?
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
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-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-
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?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-
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ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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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
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ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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first step in the aerobic pathway of viamin B12 biosynthesis
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?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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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
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-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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-
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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
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ir
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
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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
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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
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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
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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
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?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
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?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
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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
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?
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
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the enzyme generates a hydroxy lactone intermediate
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?
additional information
?
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biosynthesis of vitamin B12
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?
additional information
?
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
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biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
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ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
Q8YHT1
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
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-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
Q8YHT1
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
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-
?
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
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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
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-
-
-
?
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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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe-S center
Fe2+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
upon handling or storing CobG preparations, the sulfur content, the A400, and the enzymatic activity drops simultaneously
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Brucella melitensis cobG is PCR-amplified, overexpression of recombinant enzyme in Escherichia coli BL21 (DE3) inducible with isopropyl-1-thio-beta-D-galactopyranoside
gene cobG heterologously expressed in Escherichia coli
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overexpressed in recombinant strains of Escherichia coli
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Pseudomonas denitrificans cobG is PCR-amplified in plasmid pCR427 and cloned into pET14b, overexpression of recombinant enzyme in Escherichia coli BL21 (DE3) inducible with isopropyl-1-thio-beta-D-galactopyranoside
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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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additional information
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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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