The mechanism of Escherichia coli tryptophan indole-lyase: substituent effects on steady-state and pre-steady-state kinetic parameters for aryl-substituted tryptophan derivatives-Reference-Cited by-同舟云学术

The mechanism of Escherichia coli tryptophan indole-lyase: substituent effects on steady-state and pre-steady-state kinetic parameters for aryl-substituted tryptophan derivatives

Published:1995-02 Issue:2 Volume:3 Page:195-205
ISSN:0968-0896
Container-title:Bioorganic & Medicinal Chemistry
language:en
Short-container-title:Bioorganic & Medicinal Chemistry

Author:

Lee Minsu,Phillips Robert S.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference37 articles.

1. The interaction of Escherichia coli Tryptophanase with Various Amino Acids and Their Analogs

2. Reactions of O-acyl-l-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase

3. Interactions of tryptophan synthase, tryptophanase, and pyridoxal phosphate with oxindolyl-L-alanine and 2,3-dihydro-L-tryptophan: support for an indolenine intermediate in tryptophan metabolism

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