Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.

Ferrari, D; Yang, L H; Miles, E W; Dunn, M F

Ferrari, D; Yang, L H; Miles, E W; Dunn, M F.

Affiliation

Ferrari D; Department of Biochemistry, University of California at Riverside, 92521, USA.

Biochemistry ; 40(25): 7421-32, 2001 Jun 26.

Article in En | MEDLINE | ID: mdl-11412095

Subject(s)

Alanine/genetics; Aspartic Acid/genetics; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Mutagenesis, Site-Directed; Tryptophan Synthase/genetics; Tryptophan Synthase/metabolism; beta-Alanine/analogs & derivatives; Allosteric Regulation/genetics; Aniline Compounds/metabolism; Benzimidazoles/metabolism; Catalysis; Deuterium/metabolism; Enzyme Activation/genetics; Hydroxylamines/metabolism; Indoles/metabolism; Kinetics; Multienzyme Complexes/antagonists & inhibitors; Pyruvic Acid/metabolism; Salmonella typhimurium/enzymology; Salmonella typhimurium/genetics; Serine/analogs & derivatives; Serine/metabolism; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Substrate Specificity/genetics; Titrimetry; Tryptophan Synthase/antagonists & inhibitors; beta-Alanine/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Tryptophan Synthase / Mutagenesis, Site-Directed / Beta-Alanine / Aspartic Acid / Alanine / Multienzyme Complexes Language: En Journal: Biochemistry Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

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