This domain is found C-terminal in a number of thiolases and their homologues. Thiolases are essential CoA-dependent enzymes in lipid metabolism. This domain folds into a four-stranded antiparallel beta-sheet with helices packed on one side. Paper describing PDB structure 1afw. [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. Paper describing PDB structure 1dlu. [2]. 10764581. Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. Modis Y, Wierenga RK;. J Mol Biol. 2000;297:1171-1182. Paper describing PDB structure 1hzp. [3]. 11278743. Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III. Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT;. J Biol Chem. 2001;276:20516-20522. Paper describing PDB structure 1m1m. [4]. 16040614. Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. Brown AK, Sridharan S, Kremer L, Lindenberg S, Dover LG, Sacchettini JC, Besra GS;. J Biol Chem. 2005;280:32539-32547. Paper describing PDB structure 1m1o. [5]. 12501183. The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Kursula P, Ojala J, Lambeir AM, Wierenga RK;. Biochemistry. 2002;41:1. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16