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
-
2.1.3.1
-
biotin
-
propionibacterium
-
shermanii
-
propionyl-coa
-
biotin-containing
-
biotin-dependent
-
carboxylases
-
freudenreichii
-
propionyl
-
carboxybiotin
-
transcarboxylation
-
biotin-binding
-
medicine
-
analysis
-
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
ECTree
Advanced search results
Systematic Name
Systematic Name on EC 2.1.3.1 - methylmalonyl-CoA carboxytransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
(S)-methylmalonyl-CoA:pyruvate carboxytransferase
A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.