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transketolase C-terminal domain-containing protein
The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site [2]. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
Transketolase, pyrimidine binding domain
This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
thiamine pyrophosphate-dependent enzyme
This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase. (from Pfam)
Transketolase, thiamine diphosphate binding domain
This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
alpha-ketoacid dehydrogenase subunit alpha/beta; dehydrogenase E1 component subunit alpha/beta
alpha-ketoacid dehydrogenase containing fused E1 component alpha and beta subunits catalyzes the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide; fused dehydrogenase E1 component subunit alpha/beta contains an N-terminal thiamine pyrophosphate-dependent alpha and C-terminal beta subunits of the E1 component of a multi-enzyme dehydrogenase complex such as branched-chain alpha-keto acid dehydrogenase, which catalyzes the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide
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