An additional serine residue at the C terminus of rhodanese destabilizes the enzyme.

Kramer, G; Ramachandiran, V; Horowitz, P; Hardesty, B

Kramer, G; Ramachandiran, V; Horowitz, P; Hardesty, B.

Affiliation

Kramer G; Department of Chemistry and Biochemistry, University of Texas at Austin, 78712, USA. g.kramer@mail.utexas.edu

Arch Biochem Biophys ; 385(2): 332-7, 2001 Jan 15.

Article in En | MEDLINE | ID: mdl-11368014

Subject(s)

Mutagenesis, Site-Directed/genetics; Serine/metabolism; Thiosulfate Sulfurtransferase/chemistry; Thiosulfate Sulfurtransferase/metabolism; Animals; Arginine/genetics; Arginine/metabolism; Cattle; Cell-Free System; Chaperonin 10/metabolism; Chaperonin 60/metabolism; Codon/genetics; Enzyme Stability/drug effects; Escherichia coli; Kinetics; Leucine/metabolism; Mutation/genetics; Protein Conformation/drug effects; Protein Denaturation/drug effects; Protein Folding; Serine/genetics; Sodium Chloride/pharmacology; Temperature; Thiosulfate Sulfurtransferase/biosynthesis; Thiosulfate Sulfurtransferase/genetics; Thiosulfates/metabolism; Urea/pharmacology

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Collection: 01-internacional Database: MEDLINE Main subject: Serine / Thiosulfate Sulfurtransferase / Mutagenesis, Site-Directed Limits: Animals Language: En Journal: Arch Biochem Biophys Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

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