The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.

Kursula, Inari; Partanen, Sanna; Lambeir, Anne Marie; Wierenga, Rik K

Kursula, Inari; Partanen, Sanna; Lambeir, Anne Marie; Wierenga, Rik K.

Affiliation

Kursula I; Department of Biochemistry and Biocenter Oulu, University of Oulu, P.O. Box 3000, FIN-90014 Oulu, Finland.

FEBS Lett ; 518(1-3): 39-42, 2002 May 08.

Article in En | MEDLINE | ID: mdl-11997014

Subject(s)

Arginine/physiology; Aspartic Acid/physiology; Triose-Phosphate Isomerase/chemistry; Triose-Phosphate Isomerase/metabolism; Trypanosoma brucei brucei/enzymology; Animals; Arginine/genetics; Aspartic Acid/genetics; Binding Sites; Catalysis; Conserved Sequence; Enzyme Stability; Hydrogen Bonding; Kinetics; Models, Chemical; Models, Molecular; Mutation; Protein Folding; Salts/chemistry; Triose-Phosphate Isomerase/genetics

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Collection: 01-internacional Database: MEDLINE Main subject: Arginine / Triose-Phosphate Isomerase / Trypanosoma brucei brucei / Aspartic Acid Limits: Animals Language: En Journal: FEBS Lett Year: 2002 Document type: Article Affiliation country: Finland Country of publication: United kingdom

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