Structure of Salmonella typhimurium OMP Synthase in a Complete Substrate Complex-Reference-Cited by-同舟云学术

Structure of Salmonella typhimurium OMP Synthase in a Complete Substrate Complex

Published:2012-05-23 Issue:22 Volume:51 Page:4397-4405
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Grubmeyer Charles¹,Hansen Michael Riis²,Fedorov Alexander A.³,Almo Steven C.³

Affiliation:

1. Department of Biochemistry and Fels Research Institute, Temple University School of Medicine, 3307 North Broad Street, Philadelphia, Pennsylvania 19140, United States

2. Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark

3. Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300083p

Reference43 articles.

1. Pyrimidine Nucleotide Biosynthesis in Animals: Genes, Enzymes, and Regulation of UMP Biosynthesis

2. Suttle, D. P., Becroft, D. M. O., and Webster, D. R. (1989) Disorders of Pyrimidine Metabolism. InThe Metabolic Basis of Inherited Disease(Scriver, C. R., Beaudet, A. L., Sly, W S., and Valle, D., Eds.)6th ed., pp1095–1126,McGraw-Hill,New York.

3. Structural Features of the Phosphoribosyl-Transferases and Their Relationship to the Human Deficiency Disorders of Purine and Pyrimidine Metabolis

4. Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene.

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