Tryptophanase from Proteus vulgaris: The conformational rearrangement in the active site, induced by the mutation of Tyrosine 72 to Phenylalanine, and its mechanistic consequences

Author:

Kulikova Vitalia V.,Zakomirdina Ludmila N.,Dementieva Irene S.,Phillips Robert S.,Gollnick Paul D.,Demidkina Tatyana V.,Faleev Nicolai G.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference48 articles.

1. Tryptophanase: structure, catalytic activities, and mechanism of action;Snell;Adv. Enzymol.,1975

2. Direct spectrophotometric assay of tryptophanase;Suelter;FEBS Lett.,1976

3. The interaction of Escherichia coli tryptophanase with various amino and their analogs. Active site mapping;Watanabe;J. Biochem.,1977

4. Synthesis of l-tryptophan from pyruvate;Nakazawa;Agric. Biol. Chem.,1972

5. Y. Asai, M. Shimada, K. Soda, Manufacture of l-5-hydroxytryptophan, Mitsui Toasu Chemicals Inc. Jpn. Kokai Tokkyo Koho JP 8283,285 (Cl. Cl 12P13/04) (25 May 1982), Appl. 80/155,883 (7 November 1980), 6 pp. (Chem. Abs. 097 (15) 125715w).

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