Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid β-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar α/β domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to α-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid β-oxidation with redox regulation.

Item Type:	Refereed Article
Keywords:	arabidopsis thaliana, 3-ketoacyl-CoA thiolase, fatty acid beta-oxidation
Research Division:	Biological Sciences
Research Group:	Plant Biology
Research Field:	Plant Physiology
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Biological Sciences
Author:	Smith, SM (Professor Steven Smith)
ID Code:	101513
Year Published:	2006
Web of Science® Times Cited:	15
Deposited By:	Plant Science
Deposited On:	2015-06-25
Last Modified:	2018-03-19
Downloads:	0