Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding.

Gomi, T; Takata, Y; Date, T; Fujioka, M; Aksamit, R R; Backlund, P S; Cantoni, G L

Gomi, T; Takata, Y; Date, T; Fujioka, M; Aksamit, R R; Backlund, P S; Cantoni, G L.

Affiliation

Gomi T; Department of Biochemistry, Toyama Medical and Pharmaceutical University Faculty of Medicine, Japan.

J Biol Chem ; 265(27): 16102-7, 1990 Sep 25.

Article in En | MEDLINE | ID: mdl-1975808

Subject(s)

Aspartic Acid; Glutamates; Hydrolases/genetics; Liver/enzymology; Mutation; NAD/metabolism; Adenosylhomocysteinase; Apoenzymes/isolation & purification; Apoenzymes/metabolism; Base Sequence; Binding Sites; Cloning, Molecular; Escherichia coli/genetics; Glutamic Acid; Hydrolases/isolation & purification; Hydrolases/metabolism; Kinetics; Molecular Sequence Data; Molecular Weight; Oligonucleotide Probes; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Aspartic Acid / Glutamates / Hydrolases / Liver / Mutation / NAD Language: En Journal: J Biol Chem Year: 1990 Document type: Article Affiliation country: Japan

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