BRENDA - Enzyme Database
show all sequences of 1.14.13.83

Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation

Heldt, D.; Lawrence, A.D.; Lindenmeyer, M.; Deery, E.; Heathcote, P.; Rigby, S.E.; Warren, M.J.; Biochem. Soc. Trans. 33, 815-819 (2005)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
the enzyme contains both a non-haem iron and an Fe-S centre
Rhodobacter capsulatus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
precorrin-3A + NADH + O2
Rhodobacter capsulatus
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-3B + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter capsulatus
-
in bacteria such as Rhodobacter capsulatus CobG is substituted by an isofunctional protein called CobZ
-
Reaction
Reaction
Commentary
Organism
precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O
reaction mechanism of CobZ
Rhodobacter capsulatus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
671939
Rhodobacter capsulatus
precorrin-3B + NAD+ + H2O
-
-
-
?
precorrin-3A + NADH + O2
the enzyme generates a hydroxy lactone intermediate
671939
Rhodobacter capsulatus
precorrin-3B + NAD+ + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
flavin
enzyme-bound
Rhodobacter capsulatus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavin
enzyme-bound
Rhodobacter capsulatus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
the enzyme contains both a non-haem iron and an Fe-S centre
Rhodobacter capsulatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
precorrin-3A + NADH + O2
Rhodobacter capsulatus
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-3B + NAD+ + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
671939
Rhodobacter capsulatus
precorrin-3B + NAD+ + H2O
-
-
-
?
precorrin-3A + NADH + O2
the enzyme generates a hydroxy lactone intermediate
671939
Rhodobacter capsulatus
precorrin-3B + NAD+ + H2O
-
-
-
?
Other publictions for EC 1.14.13.83
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
698972
Schroeder
Demonstration that CobG, the m ...
Brucella melitensis 16M, Brucella melitensis, Pseudomonas denitrificans (nomen rejiciendum)
J. Biol. Chem.
284
4796-4805
2009
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2
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14
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2
2
3
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3
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2
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3
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2
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14
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2
2
3
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2
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3
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2
2
-
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-
686660
Iida
Mechanism of the ring contract ...
Pseudomonas denitrificans (nomen rejiciendum)
FEBS J.
274
3475-3481
2007
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-
-
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2
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1
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3
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1
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1
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2
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3
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-
671939
Heldt
Aerobic synthesis of vitamin B ...
Rhodobacter capsulatus
Biochem. Soc. Trans.
33
815-819
2005
-
-
-
-
-
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-
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1
-
1
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1
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1
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2
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1
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1
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1
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1
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2
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650818
Stamford
Biosynthesis of vitamin B12: t ...
Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas denitrificans (nomen rejiciendum) G3575
Chem. Biol.
4
445-451
1997
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-
1
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1
1
2
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2
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1
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4
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1
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1
1
2
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1
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4
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3209
Roessner
Overexpression in Escherichia ...
Pseudomonas denitrificans (nomen rejiciendum)
Protein Expr. Purif.
6
155-163
1995
-
-
1
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-
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1
2
1
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1
-
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1
-
-
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2
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1
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1
1
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1
2
1
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1
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2
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15269
Scott
Biosynthesis of vitamin B12. D ...
Pseudomonas denitrificans (nomen rejiciendum)
FEBS Lett.
331
105-108
1993
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1
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2
1
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1
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2
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1
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1
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2
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15270
Debussche
Biosynthesis of the corrin mac ...
Pseudomonas denitrificans (nomen rejiciendum), Pseudomonas denitrificans (nomen rejiciendum) SC510 (RifT)
J. Bacteriol.
175
7430-7440
1993
-
-
1
-
-
1
-
-
-
1
-
4
-
2
-
-
1
-
-
-
1
-
6
-
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1
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1
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1
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4
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1
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1
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6
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