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
Crystallization
Crystallization 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.
DtsR1 is crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant
-
5S-subunit, native, with His-tag and selenomethionine-protein with His-tag. Crystallization of native 5S subunit requires addition of lithium sulfate, with in turn prevents crystallization of His-tagged subunit
-
central 12S hexameric core, in complex with substrate methylmalonyl-CoA. Structure shows two stacked trimers, and a domain duplication in the monomer
of 5S metalloenzyme subunit, free and in complex with substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. Dimer of beta8alpha8 barrels with active site cobalt ion