Information on EC 3.5.2.3 - dihydroorotase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.2.3
-
RECOMMENDED NAME
GeneOntology No.
dihydroorotase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formation of cyclic amides
-
-
-
-
hydrolysis
-
-
hydrolysis of cyclic amides
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Pyrimidine metabolism
-
-
UMP biosynthesis I
-
-
UMP biosynthesis II
-
-
UMP biosynthesis III
-
-
pyrimidine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-dihydroorotate amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-93-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NCIMB 10648
-
-
Manually annotated by BRENDA team
strain NCIMB 10648
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
PAO1 strains
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
methicillin-resistant strain, gene pyrC
UniProt
Manually annotated by BRENDA team
methicillin-resistant strain, gene pyrC
UniProt
Manually annotated by BRENDA team
strain RH lambda Zap II cDNA library, strain PC117 and 5TN; strains RH, PC117, and 5TN
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
following pyrimidine limitation of orotidine 5'-monophosphate decarboxylase mutant strain cells, dihydroorotase and dihydroorotate dehydrogenase activities double while aspartate transcarbamoylase and orotate phosphoribosyltransferase activities are slightly elevated compared to their activities in the mutant strain cells grown on excess uracil
additional information
-
the enzyme contains four histidine, one aspartate, and one post-carboxylated lysine residue, which are required for metal binding and catalytic activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
dexrazoxane + H2O
ADR-925
show the reaction diagram
-
i.e. ICRF187 or (+)-1,2-bis(3,5-dioxopiperazin-1-yl)propane, cardioprotective agent
i.e. N,N-[(1S)-1-methyl-1,2-ethanediyl]bis[N-(2-amino-2-oxoethyl)glycine], biologically active form
?
dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
?
L-carbamoyl-L-aspartate
L-dihydroorotate + H2O
show the reaction diagram
L-carbamoyl-L-aspartate + H2O
L-dihydroorotate
show the reaction diagram
L-carbamoylaspartate
L-dihydroorotate + H2O
show the reaction diagram
L-dihydroorotate + H2O
L-carbamoyl-L-aspartate
show the reaction diagram
L-dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
N-(2-amino-2-oxoethyl)-N-[(1S)-2-(3,5-dioxo-1-piperazinyl)-1-methylethyl]glycine + H2O
N,N'-[(1S)-1-methyl-1,2-ethanediyl]bis[N-(2-amino-2-oxoethyl)]glycine
show the reaction diagram
-
-
-
-
ir
N-(2-amino-2-oxoethyl)-N-[(2S)-2-(3,5-dioxo-1-piperazinyl)propyl]glycine + H2O
N,N'-[(1S)-1-methyl-1,2-ethanediyl]bis[N-(2-amino-2-oxoethyl)]glycine
show the reaction diagram
-
-
-
-
ir
N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O
show the reaction diagram
-
-
-
r
N-carbamoyl-L-aspartate
dihydroorotate
show the reaction diagram
-
-
-
r
N-carbamoyl-L-aspartate
L-dihydroorotate + H2O
show the reaction diagram
-
-
-
-
r
thio-dihydroorotate + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
L-carbamoyl-L-aspartate
L-dihydroorotate + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
binuclear metal center within the active site
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-1,2,3,6-tetrahydro-6-oxopyridine-2-carboxylic acid
-
competitive inhibitor versus dihydroorotate and thio-dihydroorotate
1,10-phenanthroline
-
-
2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylate
2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylic acid
4(R)-hydroxy-6-oxo-piperidine-2(S)-carboxylic acid
-
competitive inhibitor versus dihydroorotate and thio-dihydroorotate
4(S)-hydroxy-6-oxo-piperidine-2(S)-carboxylic acid
-
competitive inhibitor versus dihydroorotate and thio-dihydroorotate
4,6-dioxo-piperidine-2-(S)-carboxylic acid
-
most active competitive inhibitor versus dihydroorotate and thio-dihydroorotate
5-aminoorotate
5-aminoorotic acid
-
-
5-bromoorotate
5-Fluoroorotate
5-iodoorotate
5-Methylorotate
8-hydroxyquinoline
-
-
Ag2+
-
0.2 mM, 63% inhibition
cis-2-oxohexahydropyrimidine-4,6-dicarboxylate
-
-
Cu2+
-
0.2 mM, 33% inhibition
desferrioxamine
-
hypoxia causes a decrease in carbamoyl phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase expression incubated under desferrioxamine-induced HIF-1alpha accumulation detected in A293T, IMR32, colo320DM and HeLa cell lines
diethyl dicarbonate
-
strong inhibition at 1 mM, activity is restored more than 95% when the enzyme is preincubated with both 1 mM diethyl dicarbonate and 5 mM L-carbamoyl-L-aspartate
diethyldicarbonate
Furosemide
-
1 mM, 80% inhibition
Hg2+
-
0.2 mM, 87% inhibition
kaempferol
-
-
L-6-thiodihydroorotate
-
-
N-carbamoylamino acids
-
competitive inhibition
N-formylaspartate
-
competitive inhibitor
Orotate
phosphate
sulfhydryl reagents
-
-
trans-2-oxohexahydropyrimidine-4,6-dicarboxylate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dimethylsulfoxide
additional information
-
following pyrimidine limitation of orotidine 5'-monophosphate decarboxylase mutant strain cells, dihydroorotase and dihydroorotate dehydrogenase activities double while aspartate transcarbamoylase and orotate phosphoribosyltransferase activities are slightly elevated compared to their activities in the mutant strain cells grown on excess uracil
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.167
(S)-dihydroorotate
0.51 - 15
carbamoyl aspartate
0.076
dihydro-DL-orotate
-
-
0.063 - 3.03
dihydroorotate
0.285 - 6
L-carbamoyl-L-aspartate
0.015 - 2.2
L-carbamoylaspartate
0.004 - 0.45
L-dihydroorotate
1.07
N-carbamoyl-DL-aspartate
-
-
0.323 - 0.348
N-Carbamoyl-L-aspartate
0.009 - 0.03
thiodihydroorotate
additional information
carbamoyl aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.55 - 1.87
(S)-dihydroorotate
127
dihydro-DL-orotate
Escherichia coli
-
-
0.073 - 181.1
L-carbamoyl-L-aspartate
0.653
L-carbamoylaspartate
0.183 - 4.31
L-dihydroorotate
195
N-carbamoyl-DL-aspartate
Escherichia coli
-
-
1.9 - 2.48
N-Carbamoyl-L-aspartate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.2 - 13.1
(S)-dihydroorotate
1637
5.69 - 7.13
N-Carbamoyl-L-aspartate
4838
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
(S)-1,2,3,6-tetrahydro-6-oxopyridine-2-carboxylic acid
-
with thio-dihydroorotate as substrate, pH. 8.0
0.0045 - 0.102
2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylic acid
1.6
4(R)-hydroxy-6-oxo-piperidine-2(S)-carboxylic acid
-
with thio-dihydroorotate as substrate, pH. 8.0
3
4(S)-hydroxy-6-oxo-piperidine-2(S)-carboxylic acid
-
with thio-dihydroorotate as substrate, pH. 8.0
0.076 - 0.44
4,6-dioxo-piperidine-2-(S)-carboxylic acid
0.16 - 0.44
5-aminoorotate
1.46 - 2.6
5-bromoorotate
0.07 - 0.145
5-Fluoroorotate
3.5
5-iodoorotate
-
Ki above 3.5 mM, for the ring cleavage reaction; Ki above 3.5 mM, for the ring cyclization reaction
0.302 - 0.56
5-Methylorotate
0.66 - 0.95
Orotate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
Cd2+
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
0.15
Co2+
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
0.031
kaempferol
Klebsiella pneumoniae
-
pH 8.0, 25C, recombinant enzyme
0.24
Mn2+
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
0.04
myricetin
Klebsiella pneumoniae
-
pH 8.0, 25C, recombinant enzyme
3.29
Ni2+
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
200
phosphate
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
0.19
Zn2+
Klebsiella pneumoniae
A6T7D6
pH 9.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0014
-
crude extract
0.4985
-
after 356fold purification
0.68
purified recombinant detagged enzyme, pH 8.3, 25C
2.66
-
-
7.14
no addition of metal ions to culture medium, pH 9.0, 25C
10.57
presence of Mn2+ in culture medium, pH 9.0, 25C
14.46
presence of Ni2+ in culture medium, pH 9.0, 25C
18
-
L-dihydroorotate as substrate
18.3
in the biosynthetic direction
18.33
purified recombinant enzyme
18.4
in the degradative direction
22.22
presence of Mg2+ in culture medium, pH 9.0, 25C
22.79
presence of Co2+ in culture medium, pH 9.0, 25C
68
-
L-carbamoylaspartate as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
cyclisation of L-carbamoylaspartate
5.8
-
cyclisation of L-carbamoylaspartate
8.4
-
hydrolysis of L-dihydroorotate
9
hydrolysis reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.8
in the degradative direction
5 - 9
in the biosynthetic direction
5.5 - 6.9
-
synthesis reaction
7.8 - 8.5
-
hydrolysis reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
; BcDOHAse starts to unfold at temperatures greater than 70C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
37 - 60
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.72
isoelectric focusing
7.45
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
; maintained by serial passage in the peritoneal cavity of CFW mice
Manually annotated by BRENDA team
additional information
-
A293T cell, colo320DM
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37900
-
2 * 37900, SDS-PAGE
38300
-
2 * 38300, SDS-PAGE
41000
-
2 * 41000 SDS-PAGE
41720
-
calculated from amino acid sequence
43700
-
gel filtration
44000
-
1 * 44000, SDS-PAGE
44200
estimated from sequence of cDNA
45600
gel filtration and laser light scattering; gel filtration, laser light scattering
46370
2 * 46370, sequence calculation
46500
detagged recombinant enzyme, gel filtration
48000
-
gel filtration; gel filtration, pure tagged enzyme
48090
-
electrospray ionization mass spectroscopy, enzyme with hexahistidine tag; mass spectroscopy, BcDHOase with the hexahistidine tag
53000
-
gel filtration
55000
-
2 * 55000, SDS-PAGE
60700
His-SUMO-tagged recombinant enzyme, gel filtration
76000
-
ultracentrifugation
80000
gel filtration
80900
-
ultracentrifugation
82000
-
gel filtration
102000
-
gel filtration
110000
-
gel filtration
210000
-
4 * 210000, SDS-PAGE
220000
-
gel filtration
386000
-
gel filtration, enzyme-aspartate transcarbamoylase complex
498000
-
gel filtration, DHOase in complex with aspartate transcarbamoylase
500000
-
aspartate transcarbamoylase-dihydroorotase complex, gel filtration
870000
-
ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
homotetramer
-
temperature-dependent conversion to homodimer, crystallization data
monomer
multimer
tetramer
-
4 * 210000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complex of aspartate transcarbamoylase and dihydroorotase
hanging drop method, monoclinic structure has a novel cysteine ligand to the zinc that blocks the active site and functions as a cysteine switch, active site residues are located in disordered loops, which may function as a disorder-to-order entropy switch
to 2.6 A resolution. The overall tertiary structure formed from the TIM-barrel secondary structure motif is conical, with the active site residing at the base of the cone. The active site includes a binuclear Zn center, with two histidine (His59 and His61) and two asparagine (Asp151 and Asp304) residues bound to the more buried first Zn atom and two histidine (178 and231) residues and Asp151 bound to the second Zn atom. The carboxylate side group of Asp151 forms a bridge between the two Zn atoms
crystallized without ligand and in the presence of the inhibitors 2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylate and 5-fluoroorotate, hanging drop vapour diffusion method with 15-20% (w/v) polyethylene glycol 3350, 0.1 M MES (pH 6.0-6.5), 75 mM MgCl2, 150 mM KCl (with ligand) or 20-25% polyethylene glycol 3350, 0.1 M Na HEPES (pH 7) and 0.2 M NaF (without ligand)
-
hanging drop vapour diffusion method with 15-20% polyethylene glycol 3350, 0.1 M MES, pH 6.0-6.5, 75 mM MgCl2, and 150 mM KCl
-
in complex with 5-fluoroorotate, hanging drop vapour diffusion method 14-16% PEG 3350, 0.1 M MES pH 6.25, 25 mM MgCl2, 0.2 M KCl and 30% sucrose
-
in the presence of enantiomerically pure L-dihydroorotate, refined at 1.9 Angstrom resolution
-
x-ray structure
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life above 150 min
65
half-life 30 min
99
-
enzyme complex with aspartate transcarbamoylase, both activities are stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, 40% loss in activity
-
-20C, activity is stable idefinitely
-
-20C, Na HEPES, pH 7.3, 10% (v/v) glycerol
-
-20C, Tris-HCl buffer, pH 8.0
-
-70C, HEPES buffer, pH 7.4, 0.5% glycerol
-80C, Bis-Tris propane buffer, pH 7.0, 20% glycerol
-
4C, 2 months, partially purified preparation
-
4C, Na HEPES, pH 7.5
-
4C, pH 7.6, phosphate buffer 0.01 - 0.1 M, 3 days
-
4C, under nitrogen, 100 mM Tris phosphate buffer, pH 7, metal free 10 mM N-carbamoyl-DL-aspartate, at least 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; more than 95% purified by PorosHQ column
-
by chromatography on N-linked gutylamine-agarose and DEAE-Sephacel
-
by Ni-NTA chromatography and Poros Q anion-exchange column; Ni-NTA agarose column chromatography, Poros Q column chromatography, and Sephadex G-75 gel filtration
-
chromatography, gel filtration, resource-Q anion exchange column
-
DEAE-Sephacel column chromatography; recombinant protein purified to homogeneity
dihydroorotase and aspartate transcarbamoylase copurify, partially purified by anion exchange chromatography, gel filtration, hydrophobic interaction chromatography; HiTrap Q column chromatography, Hiload Superdex gel filtration, and phenyl-Superose HR column chromatography
-
from overexpressing Escherichia coli
-
His-tagged recombinant protein
-
human stromal cells
-
Mono Q column chromatography
-
N-linked butylamine-agarose column chromatography and DEAE-Sephacel column chromatography
-
partial purification
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant N-terminal His-SUMO-tagged enzyme SaPyrC from Escherichia coli strain BL21(DE3), by nickel affinity chromatography, dialysis, and His-SUMO tag cleavage through HRV 3C protease, another step of nickel affinity chromatography to remove the tag, followed by ultrafiltration, and gel filtration, to about 95% purity, method optimization, the His-SUMO tag affects enzyme activity slightly
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into expression vector pET21-DEST, expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells; overexpression in Escherichia coli BL21(DES/pLysS)
-
expressed in Escherichia coli SO1263 cells
-
expressed in Escherichia coli strain SO1263; overexpression in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli strain SO1263; overexpression in Escherichia coli strain S1263/pyrC-
-
expressed in Escherichia coli strain X7014; expression in Escherichia coli mutant strain S1263 and strain X7014
expression in Escherichia coli
expression in Escherichia coli strain BL21
expression in Escherichia coli strain S1263/pyrC-
-
expression in Escherichia coli strain X7014a
-
expression in Escherichia coli, His-tag
-
expression in Escherichia colipyrC mutant strain X7014a, genes pyrC(PA3527) and pyrC2(PA5541) can complement DHOase mutant, pyrC constitutively expressed, pyrC2 can only complement the DHOase mutant when expressed from the lacZalpha promotor
expression of yeast-hamster chimeric proteins in Escherichia coli
gene pyrC, DNA and amino acid sequence determination and analysis, sequence comparison, expression of N-terminal His-SUMO-tagged enzyme in Escherichia coli strain BL21(DE3) with an HRV 3C protease recognition site inserted between the SUMO tag and SaPyrC to allow for improved cleavage by HRV protease, method optimization
human cad promoter cloned into pGL3 basic vector
-
overproduction in transformed hamster cell line 165-23
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
with a fusion peptide containing six histidine residues at the amino terminus
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D230G
-
catalytically inactive
D230N
-
catalytically inactive
C221S/C263S/C265S/C268S
-
this quadruple mutant is relatively stable to oxidation and has kinetic parameters consistent with reported values for wild type DHO
D250A
-
less than 1% of the activity possessed by the wild type enzyme
D250E
-
reduced catalytic activity compared to wild type
D250H
-
less than 1% of the activity possessed by the wild type enzyme
D250N
-
less than 1% of the activity possessed by the wild type enzyme
D250S
-
reduced catalytic activity compared to wild type
H254N
-
less than 1% of the activity possessed by the wild type enzyme
N44A
-
less than 1% of the activity possessed by the wild type enzyme
R20K
-
reduced catalytic activity compared to wild type
R20M
-
catalytically inactive
R20Q
-
less than 1% of the activity possessed by the wild type enzyme
T109A
-
decreased activity
T109G
-
negligible activity
T109V
-
strongly decreased activity
T110A
-
negligible activity
T110S
-
strongly decreased activity
T110V
-
negligible activity
D251A
complete loss of activity
D251E
4fold increase in activity
H140A
complete loss of activity
H178A
complete loss of activity
H17A
complete loss of activity
H19A
complete loss of activity
L103A
complete loss of activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
synthesis
-
growth conditions which maintain DHOase overproduction require supplementation of Yeast Carbon Base with asparagines 5 g/l, glucose 20 g/l at pH 5.5. In this medium DHOase activity decreases with time, thus in terms of DHOase yield, the best time for harvesting cells is reached after 30 to 38 h of growth
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