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Information on EC 1.3.1.14 - dihydroorotate dehydrogenase (NAD+) Word Map on EC 1.3.1.14
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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dihydroorotate dehydrogenase (NAD+)
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(S)-dihydroorotate + NAD+ = orotate + NADH + H+
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
trans-dehydrogenation mechanism
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
ping-pong steady-state kinetic mechanism
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
ping-pong steady-state kinetic mechanism
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
electron transfer mechanism
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
PyrDI contains the dihydroorotate-binding site, but PyrDII is required for full activity in vivo. Holoenzyme joins a NAD+-reductase activity
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
ping-pong mechanism
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
detailed thermodynamic analysis, midpoint reduction potential of 2Fe-2S center -212 mV, midpoint reduction potential of FMN -298 mV
-
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
-
-
-
-
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pyrimidine metabolism
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-
Pyrimidine metabolism
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-
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(S)-dihydroorotate:NAD+ oxidoreductase
Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit [4]. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
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b-type dihydroorotate dehydrogenase
-
DHO dehydrogenase
-
-
-
-
dihydro-orotic dehydrogenase
-
-
-
-
dihydroorotate dehydrogenase
-
-
-
-
dihydrorotate dehydrogenase B
-
-
-
-
L-5,6-dihydro-orotate:NAD oxidoreductase
-
-
-
-
orotate reductase
-
-
-
-
reductase, orotate
-
-
-
-
additional information
-
family IB dihydroorotate dehydrogenase
additional information
-
family IB dihydroorotate dehydrogenase
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-
-
-
brenda
subunit PyrDb; bifunctional orotate reductase and H2O2-forming NADH oxidase
UniProt
brenda
Ehrlich ascites tumor cells
-
-
brenda
-
-
-
brenda
family IB enzyme, also contains family IA enzyme, milk fermenting bacterium
-
-
brenda
-
-
-
brenda
identical with Clostridium oroticum
-
-
brenda
obligate anaerobic soil bacterium
-
-
brenda
strain ATCC 13619
-
-
brenda
-
-
-
brenda
family IB enzyme, also contains family IA enzyme
-
-
brenda
family IB enzyme, also contains family IA enzyme; milk-fermenting bacterium
-
-
brenda
subspecies Lactococcus lactis cremoris, strain MG1363
UniProt
brenda
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(S)-dihydroorotate + 2,6-dichlorophenolindophenol
orotate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(S)-dihydroorotate + acceptor
orotate + reduced acceptor
(S)-dihydroorotate + NAD+
orotate + NADH + H+
5-fluorodihydroorotate + NAD+
5-fluoroorotate + NADH + H+
-
more active substrate for reverse reaction than orotate
-
-
r
dihydroorotate + acceptor
orotate + reduced acceptor
dihydroorotate + NAD+
orotate + NADH + H+
additional information
?
-
(S)-dihydroorotate + acceptor
orotate + reduced acceptor
-
different specific activities with potassium ferricyanide, O2, fumarate and NAD+ as electron acceptors for PyrDI and the holoenzyme
-
?
(S)-dihydroorotate + acceptor
orotate + reduced acceptor
-
fourth step in UMP-biosynthesis
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
-
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
-
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
acceptor: NAD+
-
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
mechanism and pH-dependence of reaction
-
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
-
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
-
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
anti-elimination of hydrogen from (S)-dihydroorotate
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
equilibrium favours direction of orotate reduction
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
equilibrium favours direction of orotate reduction
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
equilibrium favours direction of orotate reduction
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
equilibrium favours direction of orotate reduction
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
equilibrium favours direction of orotate reduction
orotate is identical with 4-carboxyuracil
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
?, r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
substrate is oxidized by NAD+ and oxygen
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
substrate is oxidized by NAD+ and oxygen
lipoic acid is no substitute for orotate
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
-
-
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
-
-
?
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
-
?, r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
?, r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
NAD+ as ultimate electron acceptor
-
r
(S)-dihydroorotate + NAD+
orotate + NADH + H+
-
at higher pH values reaction favours direction of dihydroorotate oxidation, whereas at lower pH values direction of orotate reduction is favoured
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r
dihydroorotate + acceptor
orotate + reduced acceptor
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acceptor: NAD+
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-
?
dihydroorotate + acceptor
orotate + reduced acceptor
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acceptor: menadione
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-
?
dihydroorotate + acceptor
orotate + reduced acceptor
acceptor: NAD+ for pyrDa gene product, fumarate for pyrDb gene product
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-
dihydroorotate + acceptor
orotate + reduced acceptor
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activity measurement in permeabilized Ehrlich ascites tumor cells, acceptor: nitroblue tetrazolium
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-
?
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
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r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
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r
dihydroorotate + NAD+
orotate + NADH + H+
-
-
breakdown of orotate
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
biosynthesis of pyrimidines
-
?
dihydroorotate + NAD+
orotate + NADH + H+
-
enzyme presumably functions mainly in the metabolic synthesis of pyrimidines
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r
dihydroorotate + NAD+
orotate + NADH + H+
-
-
-
-
?
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
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r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
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r
additional information
?
-
-
-
-
-
-
additional information
?
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not: uracil, cytosine, 5-methylcytosine, thymine as substrates
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-
additional information
?
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not: uracil, cytosine, 5-methylcytosine, thymine as substrates
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-
additional information
?
-
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3-acetylpyridine-NAD+ is a more effective oxidant for dihydroorotate than NAD+, methylene blue can serve as oxidant, but not cytochrome c
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additional information
?
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NAD+ binding domain in the beta subunit of enzyme, Cys-135 plays a catalytic role and Lys-48 is important for orienting the substrate in the active site and is able to interact with FMN
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additional information
?
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O2, fumarate, and NADP+ do not serve as electron acceptors
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additional information
?
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O2, fumarate, and NADP+ do not serve as electron acceptors
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-
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(S)-dihydroorotate + acceptor
orotate + reduced acceptor
-
fourth step in UMP-biosynthesis
-
?
dihydroorotate + NAD+
orotate + NADH + H+
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
-
breakdown of orotate
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
biosynthesis of pyrimidines
-
?
dihydroorotate + NAD+
orotate + NADH + H+
-
enzyme presumably functions mainly in the metabolic synthesis of pyrimidines
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
dihydroorotate + NAD+
orotate + NADH + H+
-
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
-
r
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iron-sulfur centre
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2FE-2S cluster
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
-
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
-
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer; iron-sulfur cluster resides on the beta subunit
4Fe-4S-center
-
two [2Fe-2S] clusters as cofactors, tightly bound to the beta subunit and located in the interface of the two dimers centered between the FMN and FAD group, Cys-226, Cys-231, Cys-234 and Cys-249 binds the iron-sulfur cluster
FAD
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flavoprotein with two different flavins, probably FAD and FMN
FAD
-
flavoprotein, ratio FAD to FMN 1:1
FAD
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flavoprotein, ratio FAD to FMN 1:1; one molecule FAD and one molecule FMN per enzyme molecule
FAD
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two molecules FAD per heterotetramer
FAD
-
two molecules FAD per heterotetramer
FAD
-
flavoprotein, ratio FAD to FMN 1:1; two molecules FAD per heterotetramer
FAD
-
FAD is located on the beta subunit; two molecules FAD per heterotetramer
FAD
-
FAD is located on the beta subunit; two tightly bound FAD per heterotetrameric enzyme, FAD is necessary for ability to use NAD+ as electron acceptor, detailed way of binding
FAD
-
1 mol/mol of subunit PyrDII; 1 mol PyrDII binds 1 mol FAD and 1 mol [2Fe-2S]
flavin
-
flavoprotein with two different flavins, probably FAD and FMN; interaction of flavin and dihydroorotate is completely dependent on cysteine
flavin
-
flavin coenzyme; flavoprotein with two different flavins, probably FAD and FMN
flavin
-
flavoprotein with two different flavins, probably FAD and FMN
flavin
-
flavoprotein with two different flavins, probably FAD and FMN; NAD+-linked flavoprotein
flavin
-
1 mol of flavin per 31 g of protein; flavoprotein with two different flavins, probably FAD and FMN
flavin
-
flavoprotein with two different flavins, probably FAD and FMN; metalloflavoprotein
FMN
-
flavoprotein with two different flavins, probably FAD and FMN
FMN
-
flavoprotein, ratio FAD to FMN 1:1
FMN
-
flavoprotein, ratio FAD to FMN 1:1; one molecule FAD and one molecule FMN per enzyme molecule
FMN
-
two molecules of FMN per heterotetramer
FMN
-
two molecules of FMN per heterotetramer
FMN
-
flavoprotein, ratio FAD to FMN 1:1; two molecules of FMN per heterotetramer
FMN
-
FMN is located on the alpha subunit; two molecules of FMN per heterotetramer
FMN
-
FMN is located on the alpha subunit; two tightly bound FMN per heterotetrameric enzyme, detailed way of binding
FMN
-
PyrDI is an FMN-containing iron-sulfur flavoprotein, 1 FMN molecule per PyrDI molecule
FMN
-
key charge-stabilizing role for Lys-48 of subunit D during reduction of FMN by dihydroorotate or by electron transfer from the 2Fe-2S center
NAD+
-
additional information
-
contains 2 mol of iron per mol of enzyme
-
additional information
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one atom of iron bound per flavin
-
additional information
-
4 g iron atoms per 124 g enzyme
-
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(R,R)-5-benzyl-3-(1-carboxy-2-phenylethyl)hydantoin
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-
(S)-5-benzyl-3-carboxymethylhydantoin
-
-
(S)-N-carboxymethyl-N'-(1-carboxy-2-phenylethyl)urea
-
-
(S,S)-5-benzyl-3-(1-carboxy-2-phenylethyl)hydantoin
-
-
(S,S)-N,N'-bis(1-carboxy-2-phenylethyl)urea
-
-
(S,S)-N-(1-carboxyethyl)-N'-(1-carboxy-2-phenylethyl)urea
-
4 mM, 20% inhibition
1,10-phenanthroline
-
1 mM, 10% inhibition
2,4-Dihydroxy-6-methyl pyrimidine
-
-
3-carboxymethylhydantoin
-
-
5-benzyl-3-(1-carboxy-2-phenylethyl)-1-methylhydantoin
-
-
5-Benzyl-3-(1-carboxy-2-phenylethyl)hydantoin
-
time-dependent irreversible inhibition at the active site, mechanism
5-Methylorotate
-
2 mM, 50% inhibition of reduction of orotate
Acriflavin
-
partial inhibition
cysteine
-
inhibitory above 7 mM
Hg2+
complete inhibition of both orotate reductase and NADH oxidase reaction
hydantoin
-
derived from alpha-amino acids, weak competitive inhibitors, compounds with a benzyl goup are better inhibitors
KCN
complete inhibition of orotate reductase reaction
N,N'-bis(carboxymethyl)urea
-
-
Na3PO4
-
0.2 M, at pH 6.5, 20% inhibition
NaCl
-
0.2 M, 55% inhibition
phosphate
-
high concentrations
Quinacrine
19.2% inhibition of orotate reductase reaction
additional information
-
not inhibited by 0.01 M arsenite
-
p-chloromercuribenzoate
complete inhibition of both orotate reductase and NADH oxidase reaction
p-chloromercuribenzoate
-
completely inhibited by 0.1 mM
p-chloromercuribenzoate
-
-
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2-mercaptoethanol
-
activates
dithiothreitol
-
activates
Mercaptoacetic acid
-
activates
thioglycolate
-
stimulating effect, but less effective than cysteine
additional information
-
not activated by L-serine or L-alanine; thiol activation involves reduction of side chain of a cysteine residue corresponding to Cys-130, which functions as a general base
-
cysteine
-
essential for assay, interaction of enzyme with orotate or dihydroorotate is dependent on cysteine, whereas NADH oxidase activity is not
cysteine
-
reaction rate increases 2fold in the presence of 2-7 mM cysteine
cysteine
-
required for activation
cysteine
-
essential for assay, interaction of enzyme with orotate or dihydroorotate is dependent on cysteine, whereas NADH oxidase activity is not; required for activation of purified enzyme, but not if crude extract is used for assay
cysteine
-
L-cysteine activates strongly, D-cysteine is also an activator, 1.8 mM L-cysteine is required at pH 8 for half-maximal activity, 10 mM for near-maximal activity
glutathione
-
stimulating effect, but less effective than cysteine
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0.044 - 0.367
(S)-dihydroorotate
0.09
L-dihydroorotate
-
pH 8, 25°C
0.0037
NADH
-
wild-type enzyme
0.027 - 1
S-dihydroorotate
0.044
(S)-dihydroorotate
-
mutant enzyme K48R
0.09
(S)-dihydroorotate
-
wild-type enzyme
0.131
(S)-dihydroorotate
-
mutant enzyme K48Q
0.195
(S)-dihydroorotate
-
mutant enzyme K48A
0.367
(S)-dihydroorotate
-
mutant enzyme K48E
0.062
NAD+
-
wild-type enzyme
0.0144
Orotate
-
mutant enzyme K48Q
0.0213
Orotate
-
wild-type enzyme
0.027
S-dihydroorotate
-
holoenzyme with 2,6-dichlorophenolindophenol
0.0317
S-dihydroorotate
-
holoenzyme with menadione
0.5 - 1
S-dihydroorotate
-
PyrDI
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0.11 - 49.3
(S)-dihydroorotate
additional information
additional information
-
0.11
(S)-dihydroorotate
-
mutant enzyme K48Q
0.12
(S)-dihydroorotate
-
mutant enzyme K48A
0.42
(S)-dihydroorotate
-
mutant enzyme K48R
0.73
(S)-dihydroorotate
-
mutant enzyme K48E
49.3
(S)-dihydroorotate
-
wild-type enzyme
22
L-dihydroorotate
-
formation of orotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
45
L-dihydroorotate
-
in presence of NAD+
0.021
NADH
-
mutant enzyme K48Q
25.7
NADH
-
wild-type enzyme
0.021
Orotate
-
mutant enzyme K48Q
3.97
Orotate
-
formation of L-dihydroorotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
25.7
Orotate
-
wild-type enzyme
additional information
additional information
-
values not per enzyme molecule, but per mol of flavin
-
additional information
additional information
-
values not per enzyme molecule, but per mol of flavin
-
additional information
additional information
-
values not per enzyme molecule, but per mol of flavin
-
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0.9
(R,R)-5-benzyl-3-(1-carboxy-2-phenylethyl)hydantoin
-
-
2.3
(S)-5-benzyl-3-carboxymethylhydantoin
-
-
0.7
(S)-N-carboxymethyl-N'-(1-carboxy-2-phenylethyl)urea
-
-
0.7
(S,S)-5-benzyl-3-(1-carboxy-2-phenylethyl)hydantoin
-
-
0.4
(S,S)-N,N'-bis(1-carboxy-2-phenylethyl)urea
-
-
4.5
3-carboxymethylhydantoin
-
-
0.6
5-benzyl-3-(1-carboxy-2-phenylethyl)-1-methylhydantoin
-
-
3.3
isopropyl hydantoin
-
-
2.6
N,N'-bis(carboxymethyl)urea
-
-
0.0206
Orotate
-
holoenzyme
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0.015
native wild type enzyme, using NAD+ as acceptor, at 30°C
0.05
recombinant wild type enzyme, using NAD+ as acceptor, at 37°C
0.06
native wild type enzyme, using 2,6-dichlorophenolindophenol as acceptor, at 30°C
5.9
recombinant wild type enzyme, using 2,6-dichlorophenolindophenol as acceptor, at 37°C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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7.5
and 6.5, NADH oxidase reaction and dihydrorotate oxidase reaction
6.5
and 7.5, NADH oxidase reaction
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5.5 - 7.8
-
pH 5.5: 13% of the activity at pH 6.5; pH 7.8: 65% of the activity at pH 6.5
6.4 - 8.9
-
below and above the turnover number decreases
6.5
70% of maximal activity, dihydrorotate oxidase reaction
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-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. lactis (strain IL1403)
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28099
-
heterotetramer 2 * 33094 and 2 * 28099 predicted from seqeuence, 2 * 38000 and 2 * 31000, SDS-PAGE
31000
-
heterotetramer 2 * 33094 and 2 * 28099 predicted from seqeuence, 2 * 38000 and 2 * 31000, SDS-PAGE
32000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
33094
-
heterotetramer 2 * 33094 and 2 * 28099 predicted from seqeuence, 2 * 38000 and 2 * 31000, SDS-PAGE
34120
deduced from sequence of cDNA
38000
-
heterotetramer 2 * 33094 and 2 * 28099 predicted from seqeuence, 2 * 38000 and 2 * 31000, SDS-PAGE
85000
-
native molecular mass of PyrDI
114000
-
gel filtration; molecular mass of the holoenzyme, calculated mass 122400 Da
120000
-
analytical gel filtration
28000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
28000
-
2 * 33000 + 2 * 28000
28000
-
2 * 28000 + 2 * 33000
33000
-
2 * 33000 + 2 * 28000
33000
-
2 * 28000 + 2 * 33000
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homotetramer
-
4 * 30000-31000, guanidine treatment
heterotetramer
-
alpha2,beta2; alpha subunit is named PyrDB, beta subunit is named PyrK
heterotetramer
-
alpha subunit is named PyrDB, beta subunit is named PyrK
heterotetramer
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
heterotetramer
-
alpha2,beta2, family IB enzyme; alpha subunit is named PyrDB, beta subunit is named PyrK
heterotetramer
-
alpha2,beta2, alpha subunit with 331 amino acid residues, beta subunit with 262 amino acid residues, two closely interacting PyrDB-PyrK dimers; alpha subunit is named PyrDB, beta subunit is named PyrK
tetramer
-
2 * 33000 + 2 * 28000; heterotetramer 2 * 33094 and 2 * 28099 predicted from seqeuence, 2 * 38000 and 2 * 31000, SDS-PAGE
tetramer
2 * subunit PyrDb plus 2 * subunit PyrK
tetramer
-
2 * 28000 + 2 * 33000
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hanging-drop vapor diffusion
-
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6.5
-
more stable than at pH 7.0
390562
7
-
less stable than at pH 6.5
390562
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dithiothreitol stabilizes
-
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-18°C, prepared enzyme, that is a yellow powder, several weeks, stable
-
-20°C, 0.27 M sodium phosphate, pH 6.3, over 6 months, less than 15% loss of activity
-
4°C, crystals, over a month, little or no loss of activity
-
4°C, holoenzyme, stable for many days
-
above 20°C, 0.2 M phosphate buffer, fast loss of activity
-
on ice at room temperature, PyrDI, gradually loses activity over a period of hours
-
room temperature, holoenzyme, stable for many hours
-
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about 90fold purification
-
anion-exchange, gel filtration
-
-
-
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; expression in Escherichia coliBL21 DE3, expression of pyrDI alone and coexpression with pyrDII
-
expressed in Escherichia coli strain MC1061; two different genes
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
-
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
-
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C220A
-
pyrDII mutant, conserved, essential for activity
C225A
-
pyrDII mutant conserved, essential for activity
C228A
-
pyrDII mutant conserved, essential for activity
C230A
-
pyrDII mutant nonconserved
C243A
-
pyrDII mutant conserved, essential for activity
K48A
-
KM-value for dihydroorotate is 2.2fold higher than wild-type value, kcat is 411fold lower than wild-type value
K48E
-
KM-value for dihydroorotate is 4.1fold higher than wild-type value, kcat is 67.5fold lower than wild-type value
K48Q
-
KM-value for dihydroorotate is 1.5fold higher than wild-type value, kcat is 448fold lower than wild-type value
K48R
-
KM-value for dihydroorotate is 2fold lower than wild-type value, kcat is 117fold lower than wild-type value
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activity can be recovered by mixing the purified subunits; PyrDII-containing inclusion bodies are denatured and refolded through dialysis into buffer
-
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pharmacology
-
drug design based upon selective enzyme inhibition
medicine
-
enzyme is a part of the pyrimidine biosynthesis pathway and plays a role as target for the chemotherapy of parasitic and neoplastic diseases
nutrition
-
applications in the dairy industry
nutrition
-
applications in the dairy industry
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Friedmann, H.C.; Vennesland, B.
Purification and properties of diihydroorotic dehydrogenase
J. Biol. Chem.
233
1398-1406
1958
Faecalicatena orotica
brenda
Lieberman, I.; Kornberg, A.
Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase
Biochim. Biophys. Acta
12
223-234
1953
Faecalicatena orotica
brenda
Blattmann, P.; Retey, J.
Stereospecificity of the dihydroorotate-dehydrogenase reaction
Eur. J. Biochem.
30
130-137
1972
Faecalicatena orotica
brenda
Friedmann, H.C.; Krakow, G.
Bestimmung mit Dihydroorotat-Dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
2010-2014
1984
Faecalicatena orotica
-
brenda
Buntain, I.G.; Suckling, C.J.; Wood, H.C.S.
Latent Inhibitors. Part 4. Irreversible inhibition of dihydro-orotate dehydrogenase by hydantoins derived from amino acids
J. Chem. Soc. Perkin Trans. I
1988
3175-3182
1988
Faecalicatena orotica
-
brenda
Friedmann, H.C.; Vennesland, B.
Crystalline dihydroorotic dehydrogenase
J. Biol. Chem.
235
1526-1530
1960
Faecalicatena orotica
brenda
Nelson, C.A.; Handler, P.
Preparation of bovine xanthine oxidase and the subunit structures of some iron flavoproteins
J. Biol. Chem.
243
5368-5373
1968
Faecalicatena orotica
brenda
Argyrou, A.; Washabaugh, M.W.; Pickart, C.M.
Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
Biochemistry
39
10373-10384
2000
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
brenda
Rowland, P.; Norager, S.; Jensen, K.F.; Larsen, S.
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster
Structure
8
1227-1238
2000
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
brenda
Andersen, P.S.; Jansen, P.J.G.; Hammer, K.
Two different dihydroorotate dehydrogenases in Lactococcus lactis
J. Bacteriol.
176
3975-3982
1994
Lactococcus lactis (A2RJT9), Lactococcus lactis
brenda
Kahler, A.E.; Nielsen, F.S.; Switzer, R.L.
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits
Arch. Biochem. Biophys.
371
191-201
1999
Bacillus subtilis, Mus musculus
brenda
Marcinkeviciene, J.; Tinney, L.M.; Wang, K.H.; Rogers, M.J.; Copeland, R.A.
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
Biochemistry
38
13129-13137
1999
Enterococcus faecalis
brenda
Mohsen, A.W.; Rigby, S.E.; Jensen, K.F.; Munro, A.W.; Scrutton, N.S.
Thermodynamic basis of electron transfer in dihydroorotate dehydrogenase B from Lactococcus lactis: analysis by potentiometry, EPR spectroscopy, and ENDOR spectroscopy
Biochemistry
43
6498-6510
2004
Lactococcus lactis
brenda
Combe, J.P.; Basran, J.; Hothi, P.; Leys, D.; Rigby, S.E.; Munro, A.W.; Scrutton, N.S.
Lys-D48 is required for charge stabilization, rapid flavin reduction, and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis
J. Biol. Chem.
281
17977-17988
2006
Lactococcus lactis
brenda
Kawasaki, S.; Satoh, T.; Todoroki, M.; Niimura, Y.
b-Type dihydroorotate dehydrogenase is purified as a H2O2-forming NADH oxidase from Bifidobacterium bifidum
Appl. Environ. Microbiol.
75
629-636
2009
Bifidobacterium bifidum (B7X933), Bifidobacterium bifidum
brenda
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