Allosteric regulation and substrate channeling in multifunctional pyrimidine biosynthetic complexes: analysis of isolated domains and yeast-mammalian chimeric proteins-Reference-Cited by-同舟云学术

Allosteric regulation and substrate channeling in multifunctional pyrimidine biosynthetic complexes: analysis of isolated domains and yeast-mammalian chimeric proteins

Published:1998-08 Issue:2 Volume:281 Page:363-377
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Serre Valérie,Guy Hedeel,Liu Xin,Penverne Bernadette,Hervé Guy,Evans David

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference63 articles.

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3. In situ behavior of the pyrimidine pathway enzymes is Saccharomyces cerevisiae. 2. Reaction mechanism of aspartate transcarbamylase dissociated from carbamyl phosphate synthase by genetic alteration;Belkaı̈d;Arch. Biochem. Biophys.,1987

4. In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 3. Catalytic and regulatory properties of carbamyl phosphate synthetase;Belkaı̈d;Arch. Biochem. Biophys.,1988

5. The overall synthesis of l-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells;Christopherson;J. Biol. Chem.,1980

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