Biological and Structural Evaluation of 10R- and 10S-Methylthio-DDACTHF Reveals a New Role for Sulfur in Inhibition of Glycinamide Ribonucleotide Transformylase-Reference-Cited by-同舟云学术

Biological and Structural Evaluation of 10R- and 10S-Methylthio-DDACTHF Reveals a New Role for Sulfur in Inhibition of Glycinamide Ribonucleotide Transformylase

Published:2013-07-19 Issue:30 Volume:52 Page:5133-5144
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Connelly Stephen¹,DeMartino Jessica K.¹,Boger Dale L.¹,Wilson Ian A.¹

Affiliation:

1. Department of Integrative Structural and Computational Biology, ‡Department of Chemistry, and §The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi4005182

Reference80 articles.

1. N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribotide transformylase in Escherichia coli.

2. Mammalian Glycinamide Ribonucleotide Transformylase

3. Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase

4. TRANSITION STATE ANALOG INHIBITORS AND ENZYME CATALYSIS

5. Evaluation of the Kinetic Mechanism of Escherichia coli Glycinamide Ribonucleotide Transformylase

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