Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry.

Jhee, K H; Yang, L H; Ahmed, S A; McPhie, P; Rowlett, R; Miles, E W

Jhee, K H; Yang, L H; Ahmed, S A; McPhie, P; Rowlett, R; Miles, E W.

Affiliation

Jhee KH; National Institutes of Health, Bethesda, Maryland 20892, USA.

J Biol Chem ; 273(19): 11417-22, 1998 May 08.

Article in En | MEDLINE | ID: mdl-9565551

Subject(s)

Tryptophan Synthase/chemistry; Aspartic Acid/chemistry; Bacterial Proteins/chemistry; Binding Sites; Glutamates/chemistry; Hydrogen-Ion Concentration; Macromolecular Substances; Mutagenesis, Site-Directed; Pyridoxal Phosphate/metabolism; Schiff Bases; Serine; Spectrum Analysis; Structure-Activity Relationship; Tryptophan/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Tryptophan Synthase Language: En Journal: J Biol Chem Year: 1998 Document type: Article Affiliation country: United States Country of publication: United States

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