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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.3.1.14
701809
b-Type dihydroorotate dehydrogenase is purified as a H2O2-forming NADH oxidase from Bifidobacterium bifidum
Appl. Environ. Microbiol.
75
629-636
2009
Bifidobacterium bifidum
19060157
1.3.1.14
390564
Bestimmung mit Dihydroorotat-Dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
2010-2014
1984
Faecalicatena orotica
-
1.3.1.14
390928
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits
Arch. Biochem. Biophys.
371
191-201
1999
Bacillus subtilis
10545205
1.3.1.14
390928
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits
Arch. Biochem. Biophys.
371
191-201
1999
Mus musculus
10545205
1.3.1.14
390566
Crystalline dihydroorotic dehydrogenase
J. Biol. Chem.
235
1526-1530
1960
Faecalicatena orotica
13825167
1.3.1.14
391244
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
Biochemistry
38
13129-13137
1999
Enterococcus faecalis
10529184
1.3.1.14
390568
Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
Biochemistry
39
10373-10384
2000
Bacillus subtilis
10956027
1.3.1.14
390568
Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
Biochemistry
39
10373-10384
2000
Faecalicatena orotica
10956027
1.3.1.14
390568
Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
Biochemistry
39
10373-10384
2000
Enterococcus faecalis
10956027
1.3.1.14
390568
Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
Biochemistry
39
10373-10384
2000
Lactococcus lactis
10956027
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