Catalytic and FAD-binding residues of mitochondrial very long chain acyl-coenzyme A dehydrogenase.

Souri, M; Aoyama, T; Cox, G F; Hashimoto, T

Souri, M; Aoyama, T; Cox, G F; Hashimoto, T.

Affiliation

Souri M; Department of Biochemistry, Shinshu University School of Medicine, Matsumoto, Nagano 390, Japan. msouri@med.id.yamagata-u.ac.jp

J Biol Chem ; 273(7): 4227-31, 1998 Feb 13.

Article in En | MEDLINE | ID: mdl-9461620

Subject(s)

Acyl-CoA Dehydrogenase, Long-Chain/chemistry; Flavin-Adenine Dinucleotide/metabolism; Mitochondria, Liver/enzymology; Acyl-CoA Dehydrogenase, Long-Chain/genetics; Amino Acid Sequence; Binding Sites; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed/genetics; Palmitoyl Coenzyme A/metabolism; Phylogeny; Protein Binding; Protein Folding; Recombinant Proteins/genetics; Sequence Alignment; Trypsin/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Mitochondria, Liver / Acyl-CoA Dehydrogenase, Long-Chain / Flavin-Adenine Dinucleotide Limits: Humans Language: En Journal: J Biol Chem Year: 1998 Type: Article Affiliation country: Japan

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