Dihydrooxonate Is a Substrate of Dihydroorotate Dehydrogenase (DHOD) Providing Evidence for Involvement of Cysteine and Serine Residues in Base Catalysis-Reference-Cited by-同舟云学术

Dihydrooxonate Is a Substrate of Dihydroorotate Dehydrogenase (DHOD) Providing Evidence for Involvement of Cysteine and Serine Residues in Base Catalysis

Published:2001-07 Issue:2 Volume:391 Page:286-294
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Björnberg Olof,Jordan Douglas B.,Palfey Bruce A.,Jensen Kaj Frank

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference34 articles.

1. Active Site of Dihydroorotate Dehydrogenase A from Lactococcus lactis Investigated by Chemical Modification and Mutagenesis

2. Functional Expression of a Fragment of Human Dihydroorotate Dehydrogenase by Means of the Baculovirus Expression Vector System, and Kinetic Investigation of the Purified Recombinant Enzyme

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

4. Leflunomide: mode of action in the treatment of rheumatoid arthritis

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