BRENDA - Enzyme Database
show all sequences of 1.3.1.14

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

Combe, J.P.; Basran, J.; Hothi, P.; Leys, D.; Rigby, S.E.; Munro, A.W.; Scrutton, N.S.; J. Biol. Chem. 281, 17977-17988 (2006)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
K48A
KM-value for dihydroorotate is 2.2fold higher than wild-type value, kcat is 411fold lower than wild-type value
Lactococcus lactis
K48E
KM-value for dihydroorotate is 4.1fold higher than wild-type value, kcat is 67.5fold lower than wild-type value
Lactococcus lactis
K48Q
KM-value for dihydroorotate is 1.5fold higher than wild-type value, kcat is 448fold lower than wild-type value
Lactococcus lactis
K48R
KM-value for dihydroorotate is 2fold lower than wild-type value, kcat is 117fold lower than wild-type value
Lactococcus lactis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0037
-
NADH
wild-type enzyme
Lactococcus lactis
0.0144
-
Orotate
mutant enzyme K48Q
Lactococcus lactis
0.0213
-
Orotate
wild-type enzyme
Lactococcus lactis
0.044
-
(S)-dihydroorotate
mutant enzyme K48R
Lactococcus lactis
0.062
-
NAD+
wild-type enzyme
Lactococcus lactis
0.09
-
(S)-dihydroorotate
wild-type enzyme
Lactococcus lactis
0.131
-
(S)-dihydroorotate
mutant enzyme K48Q
Lactococcus lactis
0.195
-
(S)-dihydroorotate
mutant enzyme K48A
Lactococcus lactis
0.367
-
(S)-dihydroorotate
mutant enzyme K48E
Lactococcus lactis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactococcus lactis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
-
674586
Lactococcus lactis
orotate + NADH + H+
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.021
-
NADH
mutant enzyme K48Q
Lactococcus lactis
0.021
-
Orotate
mutant enzyme K48Q
Lactococcus lactis
0.11
-
(S)-dihydroorotate
mutant enzyme K48Q
Lactococcus lactis
0.12
-
(S)-dihydroorotate
mutant enzyme K48A
Lactococcus lactis
0.42
-
(S)-dihydroorotate
mutant enzyme K48R
Lactococcus lactis
0.73
-
(S)-dihydroorotate
mutant enzyme K48E
Lactococcus lactis
25.7
-
NADH
wild-type enzyme
Lactococcus lactis
25.7
-
Orotate
wild-type enzyme
Lactococcus lactis
49.3
-
(S)-dihydroorotate
wild-type enzyme
Lactococcus lactis
Cofactor
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
-
Lactococcus lactis
FAD
-
Lactococcus lactis
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
Lactococcus lactis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
-
Lactococcus lactis
FAD
-
Lactococcus lactis
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
Lactococcus lactis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K48A
KM-value for dihydroorotate is 2.2fold higher than wild-type value, kcat is 411fold lower than wild-type value
Lactococcus lactis
K48E
KM-value for dihydroorotate is 4.1fold higher than wild-type value, kcat is 67.5fold lower than wild-type value
Lactococcus lactis
K48Q
KM-value for dihydroorotate is 1.5fold higher than wild-type value, kcat is 448fold lower than wild-type value
Lactococcus lactis
K48R
KM-value for dihydroorotate is 2fold lower than wild-type value, kcat is 117fold lower than wild-type value
Lactococcus lactis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0037
-
NADH
wild-type enzyme
Lactococcus lactis
0.0144
-
Orotate
mutant enzyme K48Q
Lactococcus lactis
0.0213
-
Orotate
wild-type enzyme
Lactococcus lactis
0.044
-
(S)-dihydroorotate
mutant enzyme K48R
Lactococcus lactis
0.062
-
NAD+
wild-type enzyme
Lactococcus lactis
0.09
-
(S)-dihydroorotate
wild-type enzyme
Lactococcus lactis
0.131
-
(S)-dihydroorotate
mutant enzyme K48Q
Lactococcus lactis
0.195
-
(S)-dihydroorotate
mutant enzyme K48A
Lactococcus lactis
0.367
-
(S)-dihydroorotate
mutant enzyme K48E
Lactococcus lactis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
-
674586
Lactococcus lactis
orotate + NADH + H+
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.021
-
NADH
mutant enzyme K48Q
Lactococcus lactis
0.021
-
Orotate
mutant enzyme K48Q
Lactococcus lactis
0.11
-
(S)-dihydroorotate
mutant enzyme K48Q
Lactococcus lactis
0.12
-
(S)-dihydroorotate
mutant enzyme K48A
Lactococcus lactis
0.42
-
(S)-dihydroorotate
mutant enzyme K48R
Lactococcus lactis
0.73
-
(S)-dihydroorotate
mutant enzyme K48E
Lactococcus lactis
25.7
-
NADH
wild-type enzyme
Lactococcus lactis
25.7
-
Orotate
wild-type enzyme
Lactococcus lactis
49.3
-
(S)-dihydroorotate
wild-type enzyme
Lactococcus lactis
Other publictions for EC 1.3.1.14
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)
701809
Kawasaki
b-Type dihydroorotate dehydrog ...
Bifidobacterium bifidum
Appl. Environ. Microbiol.
75
629-636
2009
-
-
-
-
-
-
4
-
-
-
1
-
-
4
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
674586
Combe
Lys-D48 is required for charge ...
Lactococcus lactis
J. Biol. Chem.
281
17977-17988
2006
-
-
-
-
4
-
-
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
3
-
-
-
-
-
-
3
-
4
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
654759
Mohsen
Thermodynamic basis of electro ...
Lactococcus lactis
Biochemistry
43
6498-6510
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390568
Argyrou
Dihydroorotate dehydrogenase f ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Biochemistry
39
10373-10384
2000
6
-
2
-
-
-
-
2
4
-
3
3
-
4
-
-
1
3
-
-
1
1
13
3
1
-
-
3
-
1
-
12
-
-
-
6
-
2
12
-
-
-
-
-
-
2
4
-
3
3
-
-
-
1
-
-
1
1
13
3
1
-
-
3
-
1
-
-
-
-
-
-
-
-
390569
Rowland
Structure of dihydroorotate de ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Structure
8
1227-1238
2000
-
5
-
1
-
-
-
-
4
-
-
3
-
4
-
-
1
1
-
-
-
-
11
3
-
-
-
-
-
-
-
12
-
-
-
-
5
-
12
1
-
-
-
-
-
-
4
-
-
3
-
-
-
1
-
-
-
-
11
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390928
Kahler
Biochemical characterization o ...
Bacillus subtilis, Mus musculus
Arch. Biochem. Biophys.
371
191-201
1999
-
-
1
-
5
-
1
3
-
-
8
1
-
2
-
-
1
1
1
-
-
3
5
1
-
-
-
-
-
-
-
3
2
-
-
-
-
1
3
-
5
-
-
1
2
3
-
-
8
1
-
-
-
1
1
-
-
3
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391244
Marcinkeviciene
Dihydroorotate dehydrogenase B ...
Enterococcus faecalis
Biochemistry
38
13129-13137
1999
-
-
-
-
-
-
-
-
-
-
3
-
-
3
-
-
1
1
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390917
Andersen
Two different dihydroorotate d ...
Lactococcus lactis
J. Bacteriol.
176
3975-3982
1994
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390565
Buntain
-
Latent Inhibitors. Part 4. Irr ...
Faecalicatena orotica
J. Chem. Soc. Perkin Trans. I
1988
3175-3182
1988
-
2
-
-
-
1
12
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
8
-
-
-
2
-
1
-
-
1
-
12
8
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
390564
Friedmann
-
Bestimmung mit Dihydroorotat-D ...
Faecalicatena orotica
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
2010-2014
1984
1
-
-
-
-
-
4
2
-
-
-
-
-
1
-
-
1
-
-
-
-
1
3
-
-
-
-
1
1
-
-
4
1
-
-
1
-
-
4
-
-
-
-
4
1
2
-
-
-
-
-
-
-
1
-
-
-
1
3
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
390563
Blattmann
Stereospecificity of the dihyd ...
Faecalicatena orotica
Eur. J. Biochem.
30
130-137
1972
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
1
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390567
Nelson
Preparation of bovine xanthine ...
Faecalicatena orotica
J. Biol. Chem.
243
5368-5373
1968
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390566
Friedmann
Crystalline dihydroorotic dehy ...
Faecalicatena orotica
J. Biol. Chem.
235
1526-1530
1960
1
-
-
1
-
-
5
-
-
-
1
-
-
1
-
-
1
-
-
-
1
1
2
-
2
-
-
1
1
-
-
4
-
-
-
1
-
-
4
1
-
-
-
5
-
-
-
-
1
-
-
-
-
1
-
-
1
1
2
-
2
-
-
1
1
-
-
-
-
-
-
-
-
-
390561
Friedmann
Purification and properties of ...
Faecalicatena orotica
J. Biol. Chem.
233
1398-1406
1958
3
-
-
-
-
-
5
2
-
-
-
1
-
1
-
-
1
-
-
-
1
-
5
-
-
-
-
1
-
-
-
3
-
-
-
3
-
-
3
-
-
-
-
5
-
2
-
-
-
1
-
-
-
1
-
-
1
-
5
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
390562
Lieberman
Enzymic synthesis and breakdow ...
Faecalicatena orotica
Biochim. Biophys. Acta
12
223-234
1953
1
-
-
-
-
-
1
1
-
-
-
1
-
1
-
-
1
-
-
-
1
-
3
-
-
-
-
-
1
1
2
-
-
-
-
1
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
1
-
3
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-