Direct Measurement of the pKa of Aspartic Acid 26 in Lactobacillus casei Dihydrofolate Reductase: Implications for the Catalytic Mechanism-Reference-Cited by-同舟云学术

Direct Measurement of the pKa of Aspartic Acid 26 in Lactobacillus casei Dihydrofolate Reductase: Implications for the Catalytic Mechanism

Published:1999-05-27 Issue:25 Volume:38 Page:8038-8044
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Casarotto Marco G.¹,Basran Jaswir¹,Badii Ramin¹,Sze Kong-Hung¹,Roberts Gordon C. K.¹

Affiliation:

1. Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, G.P.O. Box 334 Canberra, ACT, 2601, Australia, Department of Biochemistry and Biological NMR Centre, University of Leicester, Leicester LE1 9HN, U.K., and Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi990301p

Reference36 articles.

1. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis.

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