Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the .beta.-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium-Reference-Cited by-同舟云学术

Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the .beta.-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium

Published:1992-02-01 Issue:4 Volume:31 Page:1180-1190
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Brzovic Peter S.,Kayastha Arvind M.,Miles Edith Wilson,Dunn Michael F.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00119a030

Reference56 articles.

1. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism

2. Reaction mechanism of Escherichia coli cystathionine .gamma.-synthase: direct evidence for a pyridoxamine derivative of vinylgloxylate as a key intermediate in pyridoxal phosphate dependent .gamma.-elimination and .gamma.-replacement reactions

3. SERINE DEAMINATION BY THE B PROTEIN OF ESCHERICHIA COLI TRYPTOPHAN SYNTHETASE

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