Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 from Zea mays-Reference-Cited by-同舟云学术

Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 from Zea mays

Published:2020-01-13 Issue:2 Volume:31 Page:227-233
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Norris Andrew¹^ORCID,Busch Florian¹^ORCID,Schupfner Michael²,Sterner Reinhard²,Wysocki Vicki H.¹^ORCID

Affiliation:

1. The Ohio State University, Department of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, Columbus, Ohio 43210, United States

2. University of Regensburg, Institute for Biophysics and Physical Biochemistry, Regensburg D-93053, Germany

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1021/jasms.9b00068

Reference33 articles.

1. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

2. Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex

3. The Tryptophan Synthase α2β2 Complex: A Model for Substrate Channeling, Allosteric Communication, and Pyridoxal Phosphate Catalysis

4. The Tryptophan Synthase Multienzyme Complex: Exploring Structure-Function Relationships with X-Ray Crystallography and Mutagenesis

5. A Novel Tryptophan Synthase β-Subunit from the HyperthermophileThermotoga maritima

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