Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state-Reference-Cited by-同舟云学术

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state

Published:1990-04-03 Issue:13 Volume:29 Page:3263-3277
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bystroff Christopher,Oatley Stuart J.,Kraut Joseph

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00465a018

Reference50 articles.

1. Purification and properties of Escherichia coli dihydrofolate reductase

2. Insights into Enzyme Function from Studies on Mutants of Dihydrofolate Reductase

3. Über Pterinchemie. 64. Mitteilung. Die Kristallstruktur von 6-Methyl-7,8-dihydropterin-monohydrochlorid-monohydrat

4. Dihydrofolate reductase: multiple conformations and alternative modes of substrate binding

5. Blakley, R. L. (1984) in Folates and Pterins, Vol.1, Chemistry and Biochemistry of Folates (Blakley,R. L. & Benkovic, S. J., Eds.) pp191-253, John Wiley & Sons, New York.

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