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PMID: 3331346 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?

Cold Spring Harbor symposia on quantitative biology ·Vol. 52 ·1987-00-00 ·Pages 603-13

Alber TC, Davenport RC, Giammona DA, Lolis E, Petsko GA, Ringe D

Abstract

暂无摘要

MeSH Terms

Binding Sites Carbohydrate Epimerases/genetics Catalysis Crystallography Kinetics Models, Molecular Mutation Protein Binding Protein Conformation Saccharomyces cerevisiae/enzymology,genetics Triose-Phosphate Isomerase/genetics,metabolism

Chemicals

Carbohydrate Epimerases Triose-Phosphate Isomerase

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Alber T C

Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.

Davenport R C

Giammona D A

Lolis E

Petsko G A

Ringe D

Article Info

Journal

Cold Spring Harbor symposia on quantitative biology

Abbr.

Cold Spring Harb Symp Quant Biol

ISSN

0091-7451

DOI

10.1101/sqb.1987.052.01.069

Published

1987-00-00

Pages

603-13

Language

English

Region

United States

NLM ID

1256107

Subset

Grants

NIGMS NIH HHS · GM-26788 · United States

External Links

PubMed source DOI: 10.1101/sqb.1987.052.01.069

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Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?

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