Information on EC 3.5.2.9 - 5-oxoprolinase (ATP-hydrolysing)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.2.9
-
RECOMMENDED NAME
GeneOntology No.
5-oxoprolinase (ATP-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gamma-glutamyl cycle
-
-
glutathione metabolism
-
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Glutathione metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
5-oxo-L-proline amidohydrolase (ATP-hydrolysing)
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CAS REGISTRY NUMBER
COMMENTARY hide
9075-46-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain F-137
-
-
Manually annotated by BRENDA team
strain F-137
-
-
Manually annotated by BRENDA team
wild-type plants and oxp1-1 and oxp2-2 mutants
UniProt
Manually annotated by BRENDA team
cauliflower
-
-
Manually annotated by BRENDA team
turnip
-
-
Manually annotated by BRENDA team
squash
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
cat
-
-
Manually annotated by BRENDA team
mouse, NCS strain
-
-
Manually annotated by BRENDA team
rabbit
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
strain F-1
-
-
Manually annotated by BRENDA team
strain F-1
-
-
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
strain ALA
-
-
Manually annotated by BRENDA team
radish
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar albino
strain Wistar albino
-
-
Manually annotated by BRENDA team
potato
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme is involved in the gamma-glutamyl cycle, a six-enzyme cycle that represents the primary pathway for glutathione synthesis and degradation
physiological function
comparison of the growth of 5-oxoprolinase deletion strains with wild-type strains in a variety of growth conditions does not yield any discernible phenotypes. Cells of glutamate auxotroph aco1D strain expressing OXP1 are able to grow on 5-oxoproline, although the growth is very slow
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-imidazolidone-4-carboxylate + ATP + H2O
2-imidazolidone + ADP + phosphate
show the reaction diagram
2-imidazoline-4-carboxylate + ATP + H2O
2-imidazoline-4-carboxylate + ADP + phosphate
show the reaction diagram
-
does not undergo ring cleavage, but stimulates formation of inorganic phosphate from ATP
-
-
?
2-imidazolinone-4-carboxylate + H2O
?
show the reaction diagram
-
-
-
-
?
2-oxo-5,5-dimethylthiazolidine-4-carboxylate + H2O
?
show the reaction diagram
-
-
-
-
?
2-piperidone-6-carboxylate + ATP + H2O
2-aminoadipate + phosphate + ADP
show the reaction diagram
2-thiazolinone-4-carboxylate + H2O
?
show the reaction diagram
-
-
-
-
?
3-methyl-5-oxoproline + H2O
2-amino-3-methylpentanedioic acid
show the reaction diagram
-
-
-
-
?
3-oxy-5-oxoproline + H2O
3-oxyglutamate + phosphate
show the reaction diagram
4-methyl-5-oxoproline + H2O
2-amino-4-methylpentanedioic acid
show the reaction diagram
-
-
-
-
?
4-oxy-5-oxoproline + H2O
4-oxyglutamate + phosphate
show the reaction diagram
5'-p-fluorosulfonylbenzoyladenosine + H2O
?
show the reaction diagram
-
-
-
-
?
5'-p-fluorosulfonylbenzoylinosine + H2O
?
show the reaction diagram
-
-
-
-
?
5-oxo-L-proline + ATP + 2 H2O
L-glutamate + phosphate + ADP
show the reaction diagram
-
assay at pH 7.2, 5 mM substrate, 4C, 20 min
-
-
?
5-oxo-L-proline + ATP + H2O
L-glutamate + ADP + phosphate
show the reaction diagram
assay at 30C, pH 9.5, reaction stopped by 20 microl acetic acid and heating for 5 min at 100C
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
show the reaction diagram
alpha-hydroxyglutarate lactone + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
show the reaction diagram
-
-
-
?
ATP + H2O
?
show the reaction diagram
CTP + H2O
?
show the reaction diagram
dATP + H2O
?
show the reaction diagram
DL-2-oxo-3,3-dimethylthiazolidine-4-carboxylate + H2O
?
show the reaction diagram
-
-
-
-
?
DL-cis-2-oxo-5-methyloxazolidine-4-carboxylate + H2O
DL-threonine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
?
show the reaction diagram
ITP + H2O
?
show the reaction diagram
L-2-iminothiazolidine-4-carboxylate + H2O
L-cystine
show the reaction diagram
-
-
-
-
?
L-2-oxooxazolidine-4-carboxylate + H2O + ATP
L-serine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
show the reaction diagram
L-dihydroorotate + H2O
?
show the reaction diagram
-
do not undergo ring cleavage, but stimulates formation of inorganic phosphate from ATP
-
-
?
L-trans-2-oxo-5-methyloxazolidine-4-carboxylate + H2O
L-threonine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
MgATP2- + H2O
?
show the reaction diagram
UTP + H2O
?
show the reaction diagram
XTP + H2O
?
show the reaction diagram
-
less than 5% of the activity observed with ATP
-
-
?
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
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
show the reaction diagram
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
show the reaction diagram
O14841
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
promotes activity significantly
Co2+
-
promotes activity significantly
FeSO4
-
1 mM , relative activity 113%
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-methyl-5-oxo-L-proline
-
-
5-oxo-L-proline
-
inhibition of IPTase activity
DL-cis-2-oxo-5-methyloxazolidine-4-carboxylate
-
inhibition of IPTase activity
DTNB
-
could be reactivated with dithiothreitol
imidazolone carboxylate
-
-
iodoacetamide
L-2-imidazolidone-4-carboxylate
L-2-iminothiazolidine-4-carboxylate
-
inhibition of IPTase activity
L-2-oxooxazolidine-4-carboxylate
-
inhibition of IPTase activity
L-2-Oxothiazolidine-4-carboxylate
L-dihydroorotic acid
L-glutamine
-
inhibition of enzyme activity in tumor tissue
L-trans-2-oxo-5-methyloxazolidine-4-carboxylate
-
inhibition of glutamate formation; inhibition of IPTase activity
-
N-bromosuccinimide
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-
N-ethylmaleimide
p-hydroxymercuribenzoate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-imidazolidone-4-carboxylate
-
5-oxoproline analog, stimulates rapid ATP cleavage, but is not hydrolyzed itself
2-piperidone-6-carboxylate
-
stimulates ATP cleavage
L-glutamine
-
enhanced enzyme activity in jejunal mucosa of tumor-bearing rats
NH2OH-HCl
-
1 mM, relative activity 109%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.0511
5-oxo-L-proline
0.0316 - 0.58
5-oxoproline
0.03 - 1
ATP
0.13 - 0.41
ITP
0.17
L-2-Oxothiazolidine-4-carboxylate
-
-
0.002
L-2-oxothiazolidine-4-carboxylic acid
0.1 - 4.2
MgATP2-
0.5
MnATP2-
-
-
0.17 - 1.11
UTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.117
5-oxo-L-proline
Rattus norvegicus
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00195
cytosolic fraction of kidney
0.625
after purification by Sepharyl S-300, Blue Sepharose and Phenyl Sepharose column chromatography
1
-
measured in tumor tissue after treatment with dietary glutamine
1.25
-
measured in jejunal mucosa in DMBA-teated rats with tumor
2.5
-
measured in tumor tissue
2.91
-
measured in jejunal mucosa in DMBA-treated rats without tumor
3
-
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats without tumor
3.6
-
-
3.75
-
measured in jejunal mucosa in normal rats
4.17
-
measured in jejunal mucosa after treatment with dietary glutamine in normal rats
4.33
-
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats with tumor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
second pH optimum at pH 9.7
7.2
-
assay at
7.8 - 8
9.7
-
second pH optimum at pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 11.3
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-
5.5 - 11.2
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
peripheral mononuclear cells
Manually annotated by BRENDA team
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normal and cancer tissues
Manually annotated by BRENDA team
-
normal and cancer tissues
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
native molecular weight, component A, gel filtration
137800
calculated from amino acid sequence
150000
SDS-PAGE
230000
-
zonal sedimentation in sucrose density gradient
260000
-
gel filtration
280000
gel filtration
325000
460000
-
gel filtration
650000
-
component B, gel filtration, native conditions
750000
-
component A, gel filtration, native conditions
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymer
tetramer
-
4 * 115000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
most stable at pH 7.5, loses activity rapidly below pH 5.5 and above pH 9
209394
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
64% initial activity retained at 60C, loses all initial activity at 70C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in absence of 5-oxo-L-proline
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, no loss of activity detected
-
-80C, no activity lost for up to 1 week
-
0C, stable for up to 2 months
-
4C, 30 mM Tris-HCl buffer pH 7.8, 10 mM potassium chloride, 1 mM MgCl2, 5 mM 5-oxoproline, activity decreases to about 60% of its initial value after 2 days, 42% after 4 days and 40% after 5-6 days, addition of dithiothreitol leads to 104% of initial activity
-
4C, loses progressively activity, 60% initial activity lost in 6 days, activity completely restored upon addition of 5 mM dithiothreitol
-
4C, up to 30 h without decrease in activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
separate purification of components A and B
-
Sepharyl S-300 gel filtration, Blue Sepharose and Phenyl Sepharose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amino acid sequence determined by cDNA cloning, gene expressed in Escherichia coli
cDNA in pT7-7, subcloned into mammalian expression vector pRc/CMV, transfected into MCF7
-
expression in Saccharamyces cerevisiae, N-terminally His-tagged
genotyping
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1241V
-
naturally occuring mutation, leading to 5-oxoprolinase deficiency
G860R
-
naturally occuring mutation, leading to 5-oxoprolinase deficiency
S323R
-
naturally occuring mutation, leading to 5-oxoprolinase deficiency
V1089I
-
naturally occuring mutation, not involved into 5-oxoprolinase deficiency
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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