Information on EC 1.5.1.2 - pyrroline-5-carboxylate reductase

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

EC NUMBER
COMMENTARY hide
1.5.1.2
-
RECOMMENDED NAME
GeneOntology No.
pyrroline-5-carboxylate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-arginine degradation VI (arginase 2 pathway)
-
-
L-ornithine degradation II (Stickland reaction)
-
-
L-proline biosynthesis I
-
-
L-proline biosynthesis II (from arginine)
-
-
L-proline biosynthesis III
-
-
Metabolic pathways
-
-
proline metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:NAD(P)+ 5-oxidoreductase
Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-17-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
blowfly
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC 7120
-
-
-
Manually annotated by BRENDA team
peanut
-
-
Manually annotated by BRENDA team
dahl
-
-
Manually annotated by BRENDA team
Chinese hamster, CHO and CHL cells
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild type and mutant flies
-
-
Manually annotated by BRENDA team
camel
-
-
Manually annotated by BRENDA team
lupin
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
garden bean
-
-
Manually annotated by BRENDA team
foxtail millet, cultivar Prasad and cultivar Lepakshi
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain P2
UniProt
Manually annotated by BRENDA team
strain P2
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cowpea
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
catalyzes step 7 in the ornithine fermentation pathway
physiological function
-
treatment with oxidized low-density lipoproteins decreases the cell number per field and causes the cells to round up. Knock-down of proline oxidase via small interfering RNA further reduces viability of cancer cells treated with oxidized low-density lipoproteins, decreases oxidized low-density lipoproteins-associated reactive oxygen species generation, decreases autophagy measured via beclin-1 protein level and light-chain 3 protein-I into LC3-II conversion. Single proline oxidase overexpression is sufficient to activate autophagy. It leads to autophagosomes accumulation and increases conversion of LC3-I into LC3-II.Beclin-1 gene expression is directly dependent on proline oxidase catalytic activity, namely the generation of prloine-oxidase-dependent superoxide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-pyrroline-3-hydroxy-5-carboxylate + NAD(P)H
L-hydroxyproline + NAD(P)+
show the reaction diagram
-
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H
L-proline + NAD(P)+
show the reaction diagram
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
3,4-dehydro-DL-proline + NADPH
?
show the reaction diagram
-
-
-
-
?
3,4-dehydro-L-proline + NAD+
?
show the reaction diagram
activity assay
-
-
?
DELTA1-piperideine-6-carboxylate + NADPH
L-pipecolic acid + NADP+
show the reaction diagram
-
-
-
ir
DELTA1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
-
-
-
r
L-Pro + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
-
the enzyme plays a role as a downstream effector in p53-mediated apoptosis of renal carcinoma cells
-
-
-
L-Pro + NAD+
1-pyrroline-5-carboxylate + NADH
show the reaction diagram
L-Pro + NADP+
1-pyrroline-5-carboxylate + NADPH
show the reaction diagram
-
-
-
-
?
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
L-proline + NADP+
1-pyrroline-5-carboxylate + NADPH + H+
show the reaction diagram
L-proline benzyl ester + NAD+
L-pyrroline-5-carboxy benzyl ester + NADH
show the reaction diagram
-
24% of activity with proline
-
-
?
L-proline methyl ester + NAD+
1-pyrroline-5-carboxy methyl ester + NADH
show the reaction diagram
-
16% of activity with proline
-
-
?
L-proline t-butyl ester + NAD+
1-pyrroline-5-carboxy tert-butylester + NADH
show the reaction diagram
-
10% of activity with proline
-
-
?
L-thioproline + NAD(P)+
1-pyrroline-3-thio-5-carboxylate + NAD(P)H
show the reaction diagram
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
additional information
?
-
-
not: D-proline, L-hydroxyproline, L-azatidine-2-carboxylate, no other amino acids
-
-
-
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
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
DELTA1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
O87725
-
-
-
r
L-Pro + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
-
the enzyme plays a role as a downstream effector in p53-mediated apoptosis of renal carcinoma cells
-
-
-
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
L-proline + NADP+
1-pyrroline-5-carboxylate + NADPH + H+
show the reaction diagram
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
-
-
NAD(P)H
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ammonium acetate
-
increase of activity
Mn2+
-
activity is significantly increased in the forward reaction, optimal concentration of the cation is about 50-100 microM
NH4Cl
-
increase of activity
phosphate
-
10 mM, reaction enhancement
potassium acetate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
([[3,5-bis(trifluoromethyl)phenyl]amino]methanediyl)bis(phosphonic acid)
-
71.2% inhibition at 0.2 mM
2,3-dichlorophenylhydroxymethylenebisphosphonic acid
-
-
2-(2,3-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
-
2-(2,3-dichlorophenylamino)ethylidenebisphosphonic acid
-
-
2-(2,6-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
-
2-(2,6-dichlorophenylamino)ethylidenebisphosphonic acid
-
-
2-(3,5-di(trifluoromethyl)phenylamino)ethylidenebisphosphonic acid
-
-
2-(3,5-dichlorophenylamino)ethylidenebisphosphonic acid
-
-
2-(3,5-dimethylphenyl)-1-hydroxyethylidenebisphosphonic acid
-
-
2-(3,5-dimethylphenylamino)ethylidenebisphosphonic acid
-
-
2-(4-benzylphenylamino)ethylidenebisphosphonic acid
-
-
2-(4-chlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
-
3,5-di(trifluoromethyl)phenylaminomethylenebisphosphonic acid
-
-
3,5-dibromophenylaminomethylenebisphosphonic acid
-
-
3,5-difluorophenylaminomethylenebisphosphonic acid
-
-
3,5-dimethylphenylhydroxymethylenebisphosphonic acid
-
-
3-acetylpyridine analogue of NAD+
-
95% inhibition at 2 mM
3-carbamoylphenylaminomethylenebisphosphonic acid
-
-
3-chlorophenylaminomethylenebisphosphonic acid
-
-
4-benzylphenylaminomethylenebisphosphonic acid
-
-
4-benzylphenylhydroxymethylenebisphosphonic acid
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
90% inhibition at 0.012 mM
5,6,7,8-tetrahydro-2-naphthylaminomethylenebisphosphonic acid
-
-
CTP
-
91% inactivation at 1 mM reversible with Mg2+
cysteine
-
77% inactivation at 10 mM
D-allohydroxyproline
-
competitive inhibition
GTP
-
100% inactivation at 10 mM, reversible with Mg2+
hydroxylamine
-
-
imidazole
-
-
indan-5-ylaminomethylenebisphosphonic acid
-
-
iodoacetamide
-
complete inactivation at 1 mM
iodoacetate
-
10% inactivation at 1 mM
L-2-acetidine-4-carboxylic acid
-
50% inactivation at 2 mM
L-hydroxyproline
-
competitive inhibition
L-proline
Mn2+
-
-
N-ethylmaleimide
-
90% inhibition at 0.02 mM, inhibition can be prevented by NADH
NADPH
-
above 0.13 mM
NaHSO3
-
88% inactivation at 1 mM
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
90% inhibition at 0.008 mM, inhibition can be prevented by addition of excess dithiothreitol
phosphate
-
-
proline
pyrroline-5-carboxylate
Sodium bisulfite
-
-
stearoyl-CoA
-
competitive inhibitor of P5CR NAD(P)H-dependent thioproline dehydrogenase activity
thiazolidine-4-carboxylic acid
thio-NAD+
-
65% inactivation at 0.2 mM
thio-NADP+
-
65% inactivation at 0.2 mM
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
52% inhibition at 0.2 mM
[[(2,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
63.9% inhibition at 0.2 mM
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
[[(3,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
92.5% inhibition at 0.2 mM
[[(3,5-dibromophenyl)amino]methanediyl]bis(phosphonic acid)
-
98.4% inhibition at 0.2 mM
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
[[(3,5-dimethylphenyl)amino]methanediyl]bis(phosphonic acid)
[[(3-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
71.2% inhibition at 0.2 mM
[[(4-benzylphenyl)amino]methanediyl]bis(phosphonic acid)
-
94.5% inhibition at 0.2 mM
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
stimulation of undialyzed enzyme at 30 mM
NaCl
-
a significant increase in the P5C reductase activity is observed with increasing severity of NaCl stress (0-200 mM)
P53
-
POX is a p53-induced gene
putrescine
-
11% activation at 5 mM
spermidine
-
10% activation at 1.2 mM
spermine
-
13% activation at 1.2 mM
troglitazone
-
is found to activate the POX promoter in colon cancer cells
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.349
1-pyrroline-5-carboxylate
0.141
3,4-dehydro-L-proline
-
4.4
DELTA1-pyrroline-3-hydroxy-5-carboxylate
-
-
0.051 - 0.62
DL-pyrroline-5-carboxylate
0.12 - 50
L-proline
0.021 - 1.64
L-pyrroline-5-carboxylate
0.151 - 10.5
NAD+
0.025 - 1.55
NADH
0.093 - 3.06
NADP+
0.006 - 0.12
NADPH
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00983 - 451.7
1-pyrroline-5-carboxylate
10
3,4-dehydro-L-proline
Homo sapiens
P32322
-
212.8
L-proline
Mycobacterium tuberculosis
-
-
310.2 - 4170
NADH
13 - 137.9
NADP+
321.6 - 4000
NADPH
1270
pyrroline-5-carboxylate
Hordeum vulgare
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.32
ATP
0.0037 - 0.38
NADP+
additional information
additional information
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00078
([[3,5-bis(trifluoromethyl)phenyl]amino]methanediyl)bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
1.187
2,3-dichlorophenylhydroxymethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.488
2-(2,3-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.431
2-(2,3-dichlorophenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
1.639
2-(2,6-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.763
2-(2,6-dichlorophenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.463
2-(3,5-di(trifluoromethyl)phenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.082
2-(3,5-dichlorophenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
1.914
2-(3,5-dimethylphenyl)-1-hydroxyethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.386
2-(3,5-dimethylphenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.488
2-(4-benzylphenylamino)ethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
2.071
2-(4-chlorophenyl)-1-hydroxyethylidenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.413
3,5-di(trifluoromethyl)phenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.054
3,5-dibromophenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.719
3,5-difluorophenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
1.409
3,5-dimethylphenylhydroxymethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.547
3-carbamoylphenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
1.618
3-chlorophenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.852
4-benzylphenylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.325
4-benzylphenylhydroxymethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.684
5,6,7,8-tetrahydro-2-naphthylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
29
EDTA
Streptococcus pyogenes
-
at pH 7.5 and 37C
1.887
indan-5-ylaminomethylenebisphosphonic acid
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.00087 - 0.335
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
0.012
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.0027
[[(2,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.00088 - 0.45
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
0.00039
[[(3,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.00022
[[(3,5-dibromophenyl)amino]methanediyl]bis(phosphonic acid)
0.134
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Arabidopsis thaliana
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
0.0256 - 1.245
[[(3,5-dimethylphenyl)amino]methanediyl]bis(phosphonic acid)
0.0009
[[(3-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.00041
[[(4-benzylphenyl)amino]methanediyl]bis(phosphonic acid)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.0014 - 0.97
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.042
-
-
0.9
-
purification step supernatant, reverse reaction
1.6
purification step: soluble cell fraction
1.7
-
purification step supernatant, forward reaction
4.167
-
-
7.1
-
-
14
purification step: Ni-NTA agarose; purification step: Resource Q
21
purification step: ammonium sulfate precipitation
30
-
purification step Ni-NTA column, reverse reaction
32
purification step: Superdex 200
57
-
purification step Ni-NTA column, forward reaction
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
cofactor NADH
6.05
-
-
6.5 - 7.1
-
-
6.7 - 7.4
-
-
6.8 - 7.5
-
pyrroline-5-carboxylate reductase activity
7 - 7.5
-
-
7 - 7.6
-
-
7 - 7.5
-
-
7.2
-
activity assay
9.8 - 10.4
-
proline dehydrogenase activity
10.2
-
proline dehydrogenase activity
10.3
-
activity assay, reverse reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
pyrroline-5-carboxylate reductase activity
6 - 7
-
-
6 - 8.5
8.5
-
no proline dehydrogenase activity below pH 8.5
9.2 - 10.5
-
proline dehydrogenase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
full-length sequence is amplified from a hepatoma cell line cDNA library
Manually annotated by BRENDA team
-
fat body, muscle, gut, haemolymph, malphigian tube
Manually annotated by BRENDA team
-
distribution in bovine cornea and lens
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
monomer, SDS-PAGE
58800
-
estimated by gel fitration
94000
-
sucrose density gradient sedimentation, gel filtration
100000
-
gel filtration
125000
-
gel filtration
230000
-
gel filtration
240000
-
gel filtration
280000
-
gel filtration
284600
-
estimated by gel fitration
320000
365000
-
decamer, analysis of nondegenerated protein by native gel electrophoresis
370000
decamer, estimated by gel filtration and SDS-PAGE
additional information
-
up to 480000 kDa, quarternary structure changes drastically with buffer environment
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
multimer
octamer
polymer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.8 A resolution structure of the pyrroline-5-carboxylate reductase apo enzyme, and its ternary complex with NADPH and substrate analog at 3.1 A
-
the protein is crystallized by the hanging-drop vapor-diffusion method at 37C and diffraction data are obtained to a resolution of 2.8 A
crystal structure is determined at 2.0 A resolution, in complex with NADP+ at 2.1 A resolution
-
crystal structure is determined at 2.15 A resolution in complex with NADP+, and at 2.20 A in complex with L-proline
-
diffraction to 3.5 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
irreversible inactivation below
392131
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
96 h stable
37
-
4 h stable
65
-
15 min stable
67
-
50% inactivation after 5 min
80
half-life 30 min
90
irreversible loss of activity at 90C for 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes during purification
-
sensitive to heat and low pH
-
sorbitol stabilizes
thiol reagents stabilize
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, 50% loss of activity in 4 weeks
-
-15C, glutathione, EDTA
-
-18C, 0.15-0.2 M potassium phosphate buffer pH 7.4, 2 months
-
-20C, 1 mg protein/ml, 50% glycerol, 0.1 mM dithiothreitol, unstable
-
-20C, 50% glycerol, 0.1 mM dithiothreitol, stable for 6 months
-
-20C, inactivation in few days, unstable in the absence of NADPH
-
-70C, 50 mM triethanolamine buffer pH 7.4, 9% w/v sucrose, 1 mM EDTA, 2 mM MgCl2, 30 mM 2-mercaptoethanol
-
-80C, 1 year
-
-80C, 20 mM Caps, pH 9.4, 0.5 M NaCl, 6 months
-80C, 5% glycerol, 2 mM dithiothreitol, 1 month
-
3C, 0.1 M sodium phosphate buffer pH 7.6, 10% (NH4)2SO4, 7 days
-
4C, 50% loss of activity in 1 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes
-
ammonium sulfate precipitation, anion exchange column chromatography, and gel filtration
-
by Ni-NTA His-binding resin affinity chromatography, the N-terminal fusion partner is cleaved by enterokinase
-
copurification with proline oxidase
-
copurification with proline oxidase, both activities located on the same protein
-
copurification with thiazolidine-4-carboxylate dehydrogenase
-
homogeneity
Ni+2-NTA His-Trap resin column chromatography, and gel filtration
-
nickel affinity gel column chromatography
-
partial
using a HiTrap Ni-NTA column
using a Ni-NTA agarose, a Superdex200 and a Resource Q column
-
usung a Ni-NTA agarose, a Superdex-200 10/300 and a Resource Q column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a proline oxidase antisense vector is constructed by amplifying a part of the proline oxidase cDNA and cloning it in the mammalian expression vector pCI
-
cloned into a pMCSG7 vector, generating an expression clone of a fusion protein with an N-terminal His6-tag and a TEV protease recognition site for expression in Escherichia coli
cloned into the pET28a+ vector with a His6 tag at the N-terminus for expression in the Escherichia coli strain B834DE3
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
fusion of enzyme promotor to beta-glucuronidase
-
into a pET28a+ vector coding for a N-terminal His-tag for expression in Escherichia coli BL21DE3
into the pET30a vector for expression in Escherichia coli BL21DE3
-
proline oxidase cDNA is cloned into the pAdtrack vector, it is used to generate a recombinant adenovirus for transfection
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oxidized low-density lipoproteins upregulate proline oxidase through nuclear receptor peroxisome proliferator-activated receptor gamma
-
upregulated micro-RNA miR-23b* in renal cancer is an important regulator of POX. Ectopic overexpression of miR-23b* in normal renal cells results in striking downregulation of POX, whereas POX expression increases markedly when endogenous miR-23b* is knocked down by its antagomirs in renal cancer cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E221A
-
affinity for substrates is increased
E221G
-
insoluble protein
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding after treatment with urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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