BRENDA - Enzyme Database show
show all sequences of 1.3.98.1

Crystal structure of dihydroorotate dehydrogenase from Leishmania major

Cordeiro, A.T.; Feliciano, P.R.; Pinheiro, M.P.; Nonato, M.C.; Biochimie 94, 1739-1748 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Leishmania major
Crystallization (Commentary)
Crystallization
Organism
apo-enzyme and in complex with orotate and with fumarate, to 2.0 A, 2.5 A and 1.9 A resolution, respectively. Both orotate and fumarate bind to the same active site and exploit similar interactions, consistent with a ping-pong mechanism. Rearrangements in the conformation of the catalytic loop have direct influence on the dimeric interface
Leishmania major
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leishmania major
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + fumarate
-
724484
Leishmania major
orotate + succinate
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
two molecules per dimer in the asymmetric crystal unit
Leishmania major
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Leishmania major
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
two molecules per dimer in the asymmetric crystal unit
Leishmania major
Crystallization (Commentary) (protein specific)
Crystallization
Organism
apo-enzyme and in complex with orotate and with fumarate, to 2.0 A, 2.5 A and 1.9 A resolution, respectively. Both orotate and fumarate bind to the same active site and exploit similar interactions, consistent with a ping-pong mechanism. Rearrangements in the conformation of the catalytic loop have direct influence on the dimeric interface
Leishmania major
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + fumarate
-
724484
Leishmania major
orotate + succinate
-
-
-
?
Other publictions for EC 1.3.98.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740019
Reis
The mechanistic study of Leish ...
Leishmania major
Biochem. J.
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651-660
2016
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741111
Silva
Computational study of the mec ...
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Phys. Chem. Chem. Phys.
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18863-18871
2013
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724484
Cordeiro
Crystal structure of dihydroor ...
Leishmania major
Biochimie
94
1739-1748
2012
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723848
Liu
Structure of the putative dihy ...
Streptococcus mutans
Acta Crystallogr. Sect. F
67
182-187
2011
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724305
McDonald
Substrate binding and reactivi ...
Lactococcus lactis
Biochemistry
50
2714-2716
2011
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4
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1
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724890
Ke
Variation among Plasmodium fal ...
Saccharomyces cerevisiae
Eukaryot. Cell
10
1053-1061
2011
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1
1
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1
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725915
Ganesan
Yeast dihydroorotate dehydroge ...
Saccharomyces cerevisiae
Mol. Biochem. Parasitol.
177
29-34
2011
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710846
Cheleski
Kinetic mechanism and catalysi ...
Trypanosoma cruzi
Anal. Biochem.
399
13-22
2010
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1
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4
1
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711915
Cheleski
Novel insights for dihydroorot ...
Trypanosoma cruzi
Eur. J. Med. Chem.
45
5899-5909
2010
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11
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1
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3
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2
1
1
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1
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11
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2
1
1
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1
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700606
Pawlik
The effect of exon (19C>A) dih ...
Homo sapiens
Pharmacogenomics
10
303-309
2009
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1
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1
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684914
Pinheiro
Crystal structure of Trypanoso ...
Trypanosoma cruzi, Trypanosoma cruzi Y
Biochem. Biophys. Res. Commun.
369
812-817
2008
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1
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12
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1
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689056
Arakaki
Characterization of Trypanosom ...
Trypanosoma brucei
Mol. Microbiol.
68
37-50
2008
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2
2
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4
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4
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1
1
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696221
Inaoka
Structures of Trypanosoma cruz ...
Trypanosoma cruzi
Biochemistry
47
10881-10891
2008
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1
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1
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3
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684848
Annoura
Dihydroorotate dehydrogenase a ...
Neobodo saliens
Biochem. Biophys. Res. Commun.
358
253-258
2007
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685146
Fagan
Mechanism of flavin reduction ...
Lactococcus lactis
Biochemistry
46
4028-4036
2007
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1
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2
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2
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1
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1
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685158
Wolfe
Interaction of benzoate pyrimi ...
Lactococcus lactis
Biochemistry
46
5741-5753
2007
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1
1
2
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2
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2
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686821
Zameitat
Dihydroorotate dehydrogenase f ...
Saccharomyces cerevisiae
FEMS Yeast Res.
7
897-904
2007
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1
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1
2
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2
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2
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1
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4
-
6
1
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1
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1
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1
1
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1
1
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2
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1
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4
-
6
1
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671050
Hurt
Structure of Plasmodium falcip ...
Plasmodium falciparum
Acta Crystallogr. Sect. D
62
312-323
2006
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1
1
1
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1
1
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1
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3
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1
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2
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1
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1
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1
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1
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671092
Cordeiro
Crystallization and preliminar ...
Leishmania major
Acta Crystallogr. Sect. F
62
1049-1051
2006
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1
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2
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676289
Sariego
Genetic diversity and kinetic ...
Trypanosoma cruzi
Parasitol. Int.
55
11-16
2006
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1
1
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1
9
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3
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7
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1
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8
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14
15
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676859
Shi
Single-molecule kinetics revea ...
Lactococcus lactis
Proc. Natl. Acad. Sci. USA
103
5775-5780
2006
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676964
Feliciano
Cloning, expression, purificat ...
Leishmania major
Protein Expr. Purif.
48
98-103
2006
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1
1
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8
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2
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5
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1
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1
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8
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656285
Baldwin
High-throughput screening for ...
Plasmodium falciparum
J. Biol. Chem.
280
21847-21853
2005
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2
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13
6
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3
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2
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3
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13
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6
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2
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3
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656891
Nara
Inhibitory action of marine al ...
Trypanosoma cruzi
Parasitol. Int.
54
59-64
2005
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1
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2
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671086
Inaoka
Expression, purification and c ...
Trypanosoma cruzi
Acta Crystallogr. Sect. F
61
875-878
2005
1
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1
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675478
Annoura
The origin of dihydroorotate d ...
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Dihydroorotate dehydrogenase m ...
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Cloning and expression of the ...
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Lactococcus lactis dihydroorot ...
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A new type of dihydroorotate d ...
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Norager
E. coli dihydroorotate dehydro ...
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Dihydrooxonate is a substrate ...
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Catalytic properties of dihydr ...
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The crystal structure of Lacto ...
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Purification and characterizat ...
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Pascal
Mechanistic studies with deute ...
Crithidia fasciculata
Biochemistry
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Pascal
Purification and properties of ...
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Purification of the primary di ...
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Taylor
Biosynthetic dihydroorotate de ...
Lactobacillus delbrueckii subsp. bulgaricus
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Biosynthetic dihydroorotate de ...
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Two functionally different dih ...
Pseudomonas sp.
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