Crystallization and preliminary X-ray diffraction studies of mitochondrial short-chain delta 3,delta 2-enoyl-CoA isomerase from rat liver

J P Zeelen; R A Pauptit; R K Wierenga; W H Kunau; J K Hiltunen

doi:10.1016/0022-2836(92)90591-7

Crystallization and preliminary X-ray diffraction studies of mitochondrial short-chain delta 3,delta 2-enoyl-CoA isomerase from rat liver

J Mol Biol. 1992 Mar 5;224(1):273-5. doi: 10.1016/0022-2836(92)90591-7.

Authors

J P Zeelen¹, R A Pauptit, R K Wierenga, W H Kunau, J K Hiltunen

Affiliation

¹ European Molecular Biology Laboratory, Heidelberg, Germany.

PMID: 1548706
DOI: 10.1016/0022-2836(92)90591-7

Abstract

Crystals of short-chain delta 3,delta 2-enoyl-CoA isomerase (EC 5.3.3.8) from rat liver mitochondria have been grown using the hanging-drop vapour diffusion technique. The enoyl-CoA isomerase is an auxiliary enzyme in the beta-oxidation pathway of fatty acid metabolism, and catalyzes the isomerization of unsaturated fatty acids to produce the metabolizable delta 2-trans isomer. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 47.9, b = 118.4 and c = 164.8 A, and diffract to 3 A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Carbon-Carbon Double Bond Isomerases*
Crystallization
Dodecenoyl-CoA Isomerase
Isomerases / chemistry*
Isomerases / metabolism
Mitochondria, Liver / enzymology*
Molecular Structure
Rats
X-Ray Diffraction

Substances

Isomerases
Carbon-Carbon Double Bond Isomerases
Dodecenoyl-CoA Isomerase