OB fold (Dihydrolipoamide Acetyltransferase, E2P)
2-enoyl-CoA Hydratase; Chain A, domain 1
methylmalonyl coenzyme A carboxyltransferase
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferasecarboxytransferase [incorrect]
Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I
Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase
Carbon-13 labelled biotin--a new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions
The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity
Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study
The structure of the exocellular polysaccharide produced by the Archaeon Haloferax gibbonsii (ATCC 33959)
Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii
The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii
Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies
Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.
As annotated in Swiss-prot (P02904), this enzyme is a multienzyme, which is composed of three subunits, 1.3S, 5S, and 12S. The 1.3S subunit (PDB;1dcz, 1dd2) serves as a carrier of carboxyl group from the 12S subunit (PDB; 1on3, 1on9) to the 5S one (see [11]). The 12 subunit transfers a carboxyl group from the terminal of methyl-malonyl-CoA to the 1.3S subunit, whilst the 5S subunit transfers the carboxyl group from the carrier protein to pyruvate, producing oxalacetate (see [11]).