βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity-Reference-Cited by-同舟云学术

βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity

Published:2001-06-01 Issue:25 Volume:40 Page:7421-7432
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ferrari Davide¹,Yang Li-Hong¹,Miles Edith W.¹,Dunn Michael F.¹

Affiliation:

1. Department of Biochemistry, University of California at Riverside, Riverside, California 92521, and The National Institutes of Health, Laboratory of Biochemistry and Genetics, NIDDK, NIH, Building 8/Room 2A09, Bethesda, Maryland 20892-0830

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi002892l

Reference50 articles.

1. Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

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