Document Detail


Relationship between structure and substrate-chain-length specificity of mitochondrial very-long-chain acyl-coenzyme A dehydrogenase.
MedLine Citation:
PMID:  9839948     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) is one of four enzymes which catalyze the initial step of the mitochondrial beta-oxidation with different but overlapping substrate-chain-length specificities. A450P, a variant of VLCAD identified in a patient with VLCAD deficiency, showed abnormal substrate-chain-length specificity. Based on this mutation, we studied the relationship between the structure and substrate-chain-length specificity of VLCAD. When VLCAD was treated with trypsin, a homodimer protein of a 48-kDa polypeptide deprived of both the amino-terminal 22 amino acids and the carboxyl-terminal 145 amino acids of VLCAD was obtained. Six Ala450 variants and tryptic-VLCAD exhibited similar substrate specificities. Effects of long-chain acyl-CoA on the tryptic cleavage and changes in the catalytic properties by deprivation of the carboxyl-terminal region suggest that this region interacts with the fatty acyl moiety of long-chain acyl-CoA. Thus, both Ala450 and the carboxyl-terminal region, which are not shared by other acyl-CoA dehydrogenases, are likely to be the determinating factors in the substrate-chain-length specificity of VLCAD.
Authors:
M Souri; T Aoyama; S Yamaguchi; T Hashimoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  257     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1998 Nov 
Date Detail:
Created Date:  1998-12-22     Completed Date:  1998-12-22     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  592-8     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Shinshu University School of Medicine, Matsumoto, Nagano, Japan. msouri@med.id.yamagata-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Acyl Coenzyme A / metabolism
Acyl-CoA Dehydrogenase, Long-Chain / chemistry,  genetics,  metabolism*
Alanine / metabolism
Base Sequence
Cells, Cultured
DNA Primers
Humans
Lipid Metabolism, Inborn Errors / enzymology
Mitochondria, Liver / enzymology*
Mutagenesis, Site-Directed
Protein Conformation
Substrate Specificity
Chemical
Reg. No./Substance:
0/Acyl Coenzyme A; 0/DNA Primers; 56-41-7/Alanine; EC 1.3.99.13/Acyl-CoA Dehydrogenase, Long-Chain

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