Protein Family Models

Thiolase is reported to be structurally related to beta-ketoacyl synthase (Pfam:PF00109), and also chalcone synthase. [1]. 9402066. The 1.8 A crystal structure of the dimeric peroxisomal. 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae:. implications for substrate binding and reaction mechanism.. Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A,. Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK;. J Mol Biol 1997;273:714-728. (from Pfam)

Date:

2024-08-14

Thiolase is reported to be structurally related to beta-ketoacyl synthase (Pfam:PF00109), and also chalcone synthase. [1]. 9402066. The 1.8 A crystal structure of the dimeric peroxisomal. 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae:. implications for substrate binding and reaction mechanism.. Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A,. Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK;. J Mol Biol 1997;273:714-728. (from Pfam)

Date:

2024-08-14

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine [1]. [1]. 9482715. Crystal structure of beta-ketoacyl-acyl carrier protein synthase. II from E.coli reveals the molecular architecture of condensing. enzymes.. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y;. EMBO J 1998;17:1183-1191. (from Pfam)

Date:

2024-08-14

Gene:

fadA

Date:

2021-09-22

This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation.

Date:

2021-04-27

acetyl-CoA C-acyltransferase FadA catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed

Date:

2023-03-06

This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli.

Gene:

fadA

Date:

2024-05-28