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
-
biotin-containing
-
biotin-dependent
- carboxylases
- freudenreichii
-
propionyl
- carboxybiotin
-
transcarboxylation
-
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
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Purification
Purification on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase
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affinity chromatography on avidin-Sepharose
on chitin column beads, the intein tag is removed by auto-splicing
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radioactive labeling of Propionibacterium freudenreichii proteins is performed, analysis of the proteins by two-dimensional gel electrophoresis follows
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recombinant 5S subunit, single step purification using Intein mediated protein ligation method and cleavage from beads by dithiothreitol
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recombinant enzyme and mutant 1.3S subunit
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recombinant enzyme and mutant 1.3S subunit, affinity chromatography on avidin(monomeric)-agarose, copurification of apo and biotinylated 1.3S forms
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separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration
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the expressed 5S subunit is purified to apparent homogeneity by a single step process by using Intein mediated protein ligation method
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