Loop Residues and Catalysis in OMP Synthase-Reference-Cited by-同舟云学术

Loop Residues and Catalysis in OMP Synthase

Published:2012-05-23 Issue:22 Volume:51 Page:4406-4415
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Gary P.¹,Hansen Michael Riis²,Grubmeyer Charles¹

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

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300082s

Reference34 articles.

1. Crystal Structure of Orotate Phosphoribosyltransferase

2. The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and .alpha.-D-5-Phosphoribosyl-1-Pyrophosphate

3. A Flexible Loop at the Dimer Interface is a Part of the Active Site of the Adjacent Monomer of Escherichia coli Orotate Phosphoribosyltransferase,

4. Structure and Function of Salmonella typhimurium Orotate Phosphoribosyltransferase: Protein Complementation Reveals Shared Active Sites

5. Ternary Complex Formation and Induced Asymmetry in Orotate Phosphoribosyltransferase,

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Regulation of the pyrimidine biosynthetic pathway by lysine acetylation of E. coli OPRTase;The FEBS Journal;2022-09-02

2. Structural investigations on orotate phosphoribosyltransferase from Mycobacterium tuberculosis, a key enzyme of the de novo pyrimidine biosynthesis;Scientific Reports;2017-04-26

3. Adenine Phosphoribosyltransferase from Sulfolobus solfataricus Is an Enzyme with Unusual Kinetic Properties and a Crystal Structure that Suggests It Evolved from a 6-Oxopurine Phosphoribosyltransferase;Biochemistry;2015-03-30

4. Catalytic site interactions in yeast OMP synthase;Archives of Biochemistry and Biophysics;2014-01

5. Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5′-monophosphate;Biomolecular NMR Assignments;2013-01-12