Information on EC 1.5.1.2 - pyrroline-5-carboxylate reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, 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
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
-
-
proline metabolism
-
-
Arginine and proline metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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
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
-
UniProt
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
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
piperideine-6-carboxylate + NADH + H+
L-pipecolic acid + NAD+
show the reaction diagram
-
-
L-pipecolic acid is the sole product
-
ir
piperideine-6-carboxylate + NADPH + H+
L-pipecolic acid + NADP+
show the reaction diagram
-
-
L-pipecolic acid is the sole product
-
ir
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
NADP+
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
NaCl
stimulation of NADPH-dependent reaction, 70% stimulation at 100 mM
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+
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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
-
-
Cl-
progressive stimulation from 20-200 mM, inhibitory above
CTP
-
91% inactivation at 1 mM reversible with Mg2+
cysteine
-
77% inactivation at 10 mM
D-allohydroxyproline
-
competitive inhibition
DL-pipecolic acid
-
65% inhibition at 10mM
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
NADP+
NADPH
-
above 0.13 mM
NaHSO3
-
88% inactivation at 1 mM
NH2OH
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
Cl-
progressive stimulation by chloride ions from 20-200 mM, inhibitory above. At 100 mM, 1.8fold stimulation in presence of NADH
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
0.02 - 2.887
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 - 0.283
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
-
-
212.8
L-proline
-
-
2.972 - 4170
NADH
13 - 137.9
NADP+
1.113 - 4000
NADPH
1270
pyrroline-5-carboxylate
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50 - 470
1-pyrroline-5-carboxylate
3100 - 6350
NADH
260 - 28500
NADPH
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
0.485 - 0.704
Cl-
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
200
KCl
Arabidopsis thaliana
F4K884
cofactor NADH, pH 7.8, 35C
200
NaCl
Arabidopsis thaliana
F4K884
cofactor NADH, pH 7.8, 35C
0.032 - 1.44
NADP+
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)
Streptococcus pyogenes
-
pH 7.5-8.0, at 37C
0.00022 - 0.134
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
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
7.3
cofactor NADH
8.4
cofactor NADPH
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
cell suspension culture established from cotyledon-derived calli
Manually annotated by BRENDA team
-
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
25000
-
8 * 25000 SDS-PAGE
28112
-
10 * 28112, calculation from nucleotide sequence, SDS-PAGE
28140
-
x * 28140, calculated from SDS-PAGE
28500
-
10-12 * 28500
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
354000
gel filtration
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
dodecamer
12 * 28000, SDS-PAGE
multimer
octamer
polymer
additional information
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
-
binary complexes of PYCR1 with NADPH or proline, at 1.9 A resolution, and a ternary complex containing NADPH and a P5C/proline analog, to 1.85 A resolution. NADPH is bound to the Rossmann fold. Structures provide a model of the Michaelis complex formed during hydride transfer
-
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 structures of unliganded P5CR decamer, and its complexes with the products NAD+, NADP+, and L-proline, to 1.7, 1.85, 1.95, and 2.1 A resolution, respectively
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
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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
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expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expression in Escherichia coli
expression in Esherichia coli
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
T238A
-
mutation in conserved residue, about 10fold decrease in catalytic efficiency
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding after treatment with urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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