2.1.3.1: methylmalonyl-CoA carboxytransferase
This is an abbreviated version!
For detailed information about methylmalonyl-CoA carboxytransferase, go to the full flat file.
Word Map on EC 2.1.3.1
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2.1.3.1
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biotin
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propionibacterium
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shermanii
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propionyl-coa
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biotin-containing
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biotin-dependent
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carboxylases
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freudenreichii
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propionyl
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carboxybiotin
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transcarboxylation
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biotin-binding
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medicine
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analysis
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diagnostics
- 2.1.3.1
- biotin
- propionibacterium
- shermanii
- propionyl-coa
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biotin-containing
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biotin-dependent
- carboxylases
- freudenreichii
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propionyl
- carboxybiotin
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transcarboxylation
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biotin-binding
- medicine
- analysis
- diagnostics
Reaction
Synonyms
5S subunit of transcarboxylase, carboxyltransferase subunit of acetyl-CoA carboxylase, carboxyltransferase, methylmalonyl coenzyme A, DtsR1, MCT, methyl malonyl CoA carboxyl transferase, methylmalonyl CoA carboxyltransferase, methylmalonyl CoA-oxalacetate transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA carboxyltransferase, methylmalonyl-CoA transcarboxylase, MMC, oxalacetic transcarboxylase, transcarboxylase
ECTree
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Engineering
Engineering on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase
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A87G
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Km not significantly changed, significantly reduced kcat
M88A
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Km not significantly changed, significantly reduced kcat
M88C
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Km not significantly changed, significantly reduced kcat
M88L
M88T
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Km not significantly changed, significantly reduced kcat
M90L
additional information
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Km not significantly changed, significantly reduced kcat
M88L
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partial reaction 1: 99% loss activity, partial reaction 2: 65% loss of activity, possibly alterations in the microenvironment of the biocytin
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Km and kcat not significantly changed
M90L
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partial reaction 1: 50% loss of activity, partial reaction 2: 115% activity compared to the 1.3 wild-type enzyme
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mutant enzyme obtained by adaptation of Propionibacterium acidipropionici immobilized in a fibrous-bed bioreactor for fed-batch fermentation of glucose. Mutant shows enhanced specific activity of methylmalonyl-CoA carboxytransferase and propionyl-CoA:succinyltransferase and lower sensitivity to propionic acid inhibition. Mutant cells have a threefold increase in length and a 24% decrease in diameter
additional information
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metabolic engineering of Propionibacteriumfreudenreichii subsp. shermanii DSM 4902 for enhanced propionic acid fermentation by overexpression of pyruvate carboxylase, methylmalonyl-CoA decarboxylase, and methylmalonyl-CoA carboxyltransferase, three biotin-dependent carboxylases in the dicarboxylic acid pathway controlling the carbon fluxin the WoodWerkman cycle, from Propionibacterium acidipropionici ATCC 4875 in Propionibacterium shermani. The co-fermentation kinetics show that with more glycerol as carbon source, both the wild-type and Ps(pKPYC4) produce more propionic acid and succinic acid, but acetic acid formation is not as significantly affected, neither is the Gly/Glu ratio, metabolic flux analysis, detailed overview
additional information
Propionibacterium freudenreichii DSM 4902
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metabolic engineering of Propionibacteriumfreudenreichii subsp. shermanii DSM 4902 for enhanced propionic acid fermentation by overexpression of pyruvate carboxylase, methylmalonyl-CoA decarboxylase, and methylmalonyl-CoA carboxyltransferase, three biotin-dependent carboxylases in the dicarboxylic acid pathway controlling the carbon fluxin the WoodWerkman cycle, from Propionibacterium acidipropionici ATCC 4875 in Propionibacterium shermani. The co-fermentation kinetics show that with more glycerol as carbon source, both the wild-type and Ps(pKPYC4) produce more propionic acid and succinic acid, but acetic acid formation is not as significantly affected, neither is the Gly/Glu ratio, metabolic flux analysis, detailed overview
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additional information
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double mutant A87M and M88A