Literature DB >> 12504675

Burning fat: the structural basis of fatty acid beta-oxidation.

Jung-Ja P Kim1, Kevin P Battaile.   

Abstract

Recent advances in the structural biology of the enzymes involved in fatty acid oxidation have revealed their catalytic mechanisms and modes of substrate binding. Although these enzymes all use coenzyme A (CoA) thioesters as substrates, they share no common polypeptide folding topology or CoA-binding motif. Each family adopts an entirely unique protein fold. Their mode of binding the CoA thioester is similar in that the fatty-acyl moiety is buried inside the protein and the nucleotide portion is mainly exposed to solvent; however, the conformations of the enzyme-bound CoA ligands vary considerably. Furthermore, a comparison of these structures suggests a structural basis for the broad substrate chain length specificity that is a unique feature of these enzymes.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 12504675     DOI: 10.1016/s0959-440x(02)00390-1

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  17 in total

1.  Mycobacterium tuberculosis cholesterol catabolism requires a new class of acyl coenzyme A dehydrogenase.

Authors:  Martin I Voskuil
Journal:  J Bacteriol       Date:  2013-07-26       Impact factor: 3.490

Review 2.  Research progress and the biotechnological applications of multienzyme complex.

Authors:  Yi Jiang; Xinyi Zhang; Haibo Yuan; Di Huang; Ruiming Wang; Hongling Liu; Tengfei Wang
Journal:  Appl Microbiol Biotechnol       Date:  2021-02-10       Impact factor: 4.813

3.  Dgat1 and Dgat2 regulate enterocyte triacylglycerol distribution and alter proteins associated with cytoplasmic lipid droplets in response to dietary fat.

Authors:  Yu-Han Hung; Alicia L Carreiro; Kimberly K Buhman
Journal:  Biochim Biophys Acta Mol Cell Biol Lipids       Date:  2017-02-27       Impact factor: 4.698

4.  Shrinking the FadE proteome of Mycobacterium tuberculosis: insights into cholesterol metabolism through identification of an α2β2 heterotetrameric acyl coenzyme A dehydrogenase family.

Authors:  Matthew F Wipperman; Meng Yang; Suzanne T Thomas; Nicole S Sampson
Journal:  J Bacteriol       Date:  2013-07-08       Impact factor: 3.490

5.  Purification, crystallization and preliminary X-ray diffraction analysis of 3-ketoacyl-CoA thiolase A1887 from Ralstonia eutropha H16.

Authors:  Jieun Kim; Kyung Jin Kim
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-05-22       Impact factor: 1.056

6.  Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria.

Authors:  Irina V Perevoshchikova; Casey L Quinlan; Adam L Orr; Akos A Gerencser; Martin D Brand
Journal:  Free Radic Biol Med       Date:  2013-04-11       Impact factor: 7.376

7.  Protein-protein interactions in the β-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex.

Authors:  Andrey M Grishin; Eunice Ajamian; Linhua Zhang; Isabelle Rouiller; Mihnea Bostina; Miroslaw Cygler
Journal:  J Biol Chem       Date:  2012-09-07       Impact factor: 5.157

8.  Transcription profiling and regulation of fat metabolism genes in diapausing adults of the mosquito Culex pipiens.

Authors:  Cheolho Sim; David L Denlinger
Journal:  Physiol Genomics       Date:  2009-08-25       Impact factor: 3.107

9.  Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.

Authors:  Momoyo Ishikawa; Daisuke Tsuchiya; Takuji Oyama; Yasuo Tsunaka; Kosuke Morikawa
Journal:  EMBO J       Date:  2004-07-01       Impact factor: 11.598

10.  Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association.

Authors:  Henriette Franz; Kerstin Mosch; Szabolcs Soeroes; Henning Urlaub; Wolfgang Fischle
Journal:  J Biol Chem       Date:  2009-10-05       Impact factor: 5.157

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.