Dihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis-Reference-Cited by-同舟云学术

Dihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis

Published:2009-01-07 Issue:4 Volume:48 Page:766-778
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Zhang Pengfei¹,Martin Philip D.¹,Purcarea Cristina¹,Vaishnav Asmita¹,Brunzelle Joseph S.¹,Fernando Roshini¹,Guy-Evans Hedeel I.¹,Evans David R.¹,Edwards Brian F. P.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Street, Detroit, Michigan 48201, Department of Microbiology, Institute of Biology Bucharest, 060031 Bucharest, Romania, Life Sciences Collaborative Access Team, Northwestern University Center for Synchrotron Research, Argonne, Illinois 60439, and Department of Chemistry, Eastern Michigan University, Ypsilanti, Michigan 48197

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801831r

Reference59 articles.

1. Mammalian Pyrimidine Biosynthesis: Fresh Insights into an Ancient Pathway

2. The overall synthesis of L-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells. Kinetic studies, substrate channeling, and the effects of inhibitors.

3. A Reciprocal Allosteric Mechanism for Efficient Transfer of Labile Intermediates between Active Sites in CAD, the Mammalian Pyrimidine-Biosynthetic Multienzyme Polypeptide

4. Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells.

5. Aquifex aeolicus Aspartate Transcarbamoylase, an Enzyme Specialized for the Efficient Utilization of Unstable Carbamoyl Phosphate at Elevated Temperature

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