Protein Family Models

This entry represents the C-terminal domain found in transketolase and transketolase-like enzymes [1-5], such as pyruvate dehydrogenase E1 component (OPD1) [4]. Paper describing PDB structure 1ay0. [1]. 9398292. Identification of catalytically important residues in yeast transketolase. Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G;. Biochemistry. 1997;36:15643-15649. Paper describing PDB structure 1gpu. [2]. 11773632. Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Fiedler E, Thorell S, Sandalova T, Golbik R, Konig S, Schneider G;. Proc Natl Acad Sci U S A. 2002;99:591-595. Paper describing PDB structure 1itz. [3]. 12913150. Structure and properties of an engineered transketolase from maize. Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M;. Plant Physiol. 2003;132:1941-1949. Paper describing PDB structure 1l8a. [4]. 11955070. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W;. Biochemistry. 2002;41:5213-5221. Paper describing PDB structure 1r9j. [5]. 15149284. Transketolase from Leishmania mexicana has a dual subcellular localization. Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP;. Biochem J. 2004;382:759-767. (from Pfam)

Date:

2024-10-16

This entry represents one of the thiamin diphosphate-binding domains found in pyruvate dehydrogenase E1 component [1]. [1]. 11955070. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W;. Biochemistry. 2002;41:5213-5221. [2]. 14992577. Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Arjunan P, Chandrasekhar K, Sax M, Brunskill A, Nemeria N, Jordan F, Furey W;. Biochemistry. 2004;43:2405-2411. [3]. 16531404. A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W;. J Biol Chem. 2006;281:15296-15303. [4]. 17057342. Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution. Chandrasekhar K, Arjunan P, Sax M, Nemeria N, Jordan F, Furey W;. Acta Crystallogr D Biol Crystallogr. 2006;62:1382-1386. [5]. 17635929. A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. Kale S, Arjunan P, Furey W, Jordan F;. J Biol Chem. 2007;282:28106-28116. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

E1 component of the acetyl-transferring homodimeric-type pyruvate dehydrogenase multienzyme complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2

Date:

2023-03-13

Most members of this family are pyruvate dehydrogenase complex, E1 component. Note: this family was classified as subfamily rather than equivalog because it includes a counterexample from Pseudomonas putida, MdeB, that is active as an E1 component of an alpha-ketoglutarate dehydrogenase complex rather than a pyruvate dehydrogase complex. The second pyruvate dehydrogenase complex E1 protein from Alcaligenes eutrophus, PdhE, complements an aceE mutant of E. coli but is not part of a pyruvate dehydrogenase complex operon, is more similar to the Pseudomonas putida MdeB than to E. coli AceE, and may have also have a different primary specificity.

Gene:

aceE

Date:

2024-05-02