BRENDA - Enzyme Database
show all sequences of 1.13.11.79

BluB/CobT2 fusion enzyme activity reveals mechanisms responsible for production of active form of vitamin B12 by Propionibacterium freudenreichii

Deptula, P.; Kylli, P.; Chamlagain, B.; Holm, L.; Kostiainen, R.; Piironen, V.; Savijoki, K.; Varmanen, P.; Microb. Cell Fact. 14, 186 (2015)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene bluB/cobT2, a natural fusion gene coding for a predicted phosphoribosyltransferase/nitroreductase, sequence comparisons, recombinant expression of HaloTag-tagged enzyme in Escherichia coli strain KRX
Propionibacterium freudenreichii subsp. shermanii
Organism
Organism
UniProt
Commentary
Textmining
Propionibacterium freudenreichii subsp. shermanii
D7GJ95
-
-
Propionibacterium freudenreichii subsp. shermanii DSM 4902
D7GJ95
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant HaloTag-tagged enzyme from Escherichia coli strain KRX
Propionibacterium freudenreichii subsp. shermanii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
FMNH2 + O2
-
745700
Propionibacterium freudenreichii subsp. shermanii
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
-
-
?
FMNH2 + O2
-
745700
Propionibacterium freudenreichii subsp. shermanii DSM 4902
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
BluB
-
Propionibacterium freudenreichii subsp. shermanii
bluB/cobT2
-
Propionibacterium freudenreichii subsp. shermanii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Propionibacterium freudenreichii subsp. shermanii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bluB/cobT2, a natural fusion gene coding for a predicted phosphoribosyltransferase/nitroreductase, sequence comparisons, recombinant expression of HaloTag-tagged enzyme in Escherichia coli strain KRX
Propionibacterium freudenreichii subsp. shermanii
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant HaloTag-tagged enzyme from Escherichia coli strain KRX
Propionibacterium freudenreichii subsp. shermanii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
FMNH2 + O2
-
745700
Propionibacterium freudenreichii subsp. shermanii
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
-
-
?
FMNH2 + O2
-
745700
Propionibacterium freudenreichii subsp. shermanii DSM 4902
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Propionibacterium freudenreichii subsp. shermanii
General Information
General Information
Commentary
Organism
metabolism
BluB/CobT2 is the crucial enzyme in the B12 biosynthetic pathway of Propionibacterium freudenreichii
Propionibacterium freudenreichii subsp. shermanii
physiological function
the enzyme is involved in production of vitamin B12, a prerequisite for attempts to naturally fortify foods with B12 by microbial fermentation. Active vitamin B12 is distinguished from the pseudovitamin by the presence of 5,6-dimethylbenzimidazole (DMBI) as the lower ligand. Fusion enzyme BluB/CobT2 is efficient in metabolite channeling, and the enzymes' inability to react with adenine, a lower ligand present in the pseudovitamin, reveals a mechanism favoring the production of the active form of the vitamin, requirement of oxygen for DMBI synthesis, since the organism does not synthesize cobalamin. BluB is responsible for the formation of DMBI from FMNH2 in the presence of oxygen, BluB/CobT2 activates DMBI into alpha-RP in the presence of NaMN
Propionibacterium freudenreichii subsp. shermanii
General Information (protein specific)
General Information
Commentary
Organism
metabolism
BluB/CobT2 is the crucial enzyme in the B12 biosynthetic pathway of Propionibacterium freudenreichii
Propionibacterium freudenreichii subsp. shermanii
physiological function
the enzyme is involved in production of vitamin B12, a prerequisite for attempts to naturally fortify foods with B12 by microbial fermentation. Active vitamin B12 is distinguished from the pseudovitamin by the presence of 5,6-dimethylbenzimidazole (DMBI) as the lower ligand. Fusion enzyme BluB/CobT2 is efficient in metabolite channeling, and the enzymes' inability to react with adenine, a lower ligand present in the pseudovitamin, reveals a mechanism favoring the production of the active form of the vitamin, requirement of oxygen for DMBI synthesis, since the organism does not synthesize cobalamin. BluB is responsible for the formation of DMBI from FMNH2 in the presence of oxygen, BluB/CobT2 activates DMBI into alpha-RP in the presence of NaMN
Propionibacterium freudenreichii subsp. shermanii
Other publictions for EC 1.13.11.79
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
Synonyms
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)
745700
Deptula
BluB/CobT2 fusion enzyme acti ...
Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii DSM 4902
Microb. Cell Fact.
14
186
2015
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728590
Collins
Bacillus megaterium has both a ...
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PLoS ONE
8
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2013
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Intermediate-assisted multifun ...
Sinorhizobium meliloti
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133
4079-4091
2011
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689775
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Single-enzyme conversion of FM ...
Rhodospirillum rubrum
Proc. Natl. Acad. Sci. USA
104
2921-2926
2007
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705877
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BluB cannibalizes flavin to fo ...
Sinorhizobium meliloti
Nature
446
449-453
2007
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2007
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Sinorhizobium meliloti
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103
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2006
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