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
1.5.1.2
-
RECOMMENDED NAME
GeneOntology No.
pyrroline-5-carboxylate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenation
P32322
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
redox reaction
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
arginine degradation VI (arginase 2 pathway)
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
ornithine degradation II (Stickland reaction)
-
proline biosynthesis I
-
proline biosynthesis II (from arginine)
-
proline biosynthesis III
-
SYSTEMATIC NAME
IUBMB Comments
L-proline:NAD(P)+ 5-oxidoreductase
Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-pyrroline-5-carboxylate reductase
-
-
-
-
DELTA1-pyrroline-5-carboxylate reductase
-
-
DELTA1-pyrroline-5-carboxylate reductase
-
-
DELTA1-pyrroline-5-carboxylate reductase
-
-
DELTA1-pyrroline-5-carboxylate reductase
Streptococcus pyogenes ATCC 19615
-
-
-
L-proline oxidase
-
-
-
-
L-proline-NAD(P)+ 5-oxidoreductase
-
-
-
-
NADPH-L-DELTA'-pyrroline carboxylic acid reductase
-
-
-
-
P5C reductase
-
-
-
-
P5C reductase
-
-
P5C reductase
-
-
P5C reductase
-
-
P5C reductase
-
-
P5C reductase
-
-
P5C reductase
Streptococcus pyogenes ATCC 19615
-
-
-
P5C reductase
-
-
P5CR
-
-
-
-
P5CR
-
-
P5CR
Anabaena sp. PCC 7120
-
-
-
P5CR
-
-
P5CR
P32322
-
proline oxidase
-
-
-
-
proline oxidase
-
-
proline oxidase
-
-
pyrroline-5-carboxylate dehydrogenase
-
-
pyrroline-5-carboxylate reductase
O87725
-
pyrroline-5-carboxylate reductase
-
-
pyrroline-5-carboxylate reductase
P32322
-
pyrroline-5-carboxylate reductase
-
-
pyrroline-5-carboxylate reductase
-
-
reductase, pyrroline-5-carboxylate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-17-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Anabaena sp. PCC 7120
-
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
Chinese hamster, CHO and CHL cells
-
-
Manually annotated by BRENDA team
wild type and mutant flies
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
soybean inoculated with Bradyrhizobium japonicum
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
patients with cutis laxia type 2
A6NFM2
UniProt
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
var Larker
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
garden bean
-
-
Manually annotated by BRENDA team
male Sprague-Dawley
-
-
Manually annotated by BRENDA team
foxtail millet, cultivar Prasad and cultivar Lepakshi
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes ATCC 19615
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
O87725
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q97ZT3, -
-
-
-
r
1-pyrroline-5-carboxylate + NAD(P)H
L-proline + NAD(P)+
show the reaction diagram
Q97ZT3, -
-
-
-
r
1-pyrroline-5-carboxylate + NAD(P)H + 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 + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + 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
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + 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 + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + 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 + NAD(P)H + 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 + NAD(P)H + 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 + NAD(P)H + 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
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
reversible at pH values above 8 and higher substrate concentrations, oxidation of L-proline is strictly specific for the L-isomer
-
r
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
reaction is irreversible at pH 7.4, but reversible at pH 10.3
-
-
r
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
specific for L-isomer
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
specific for L-isomer
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
specific for L-isomer
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
specific for L-isomer
-
-
ir
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
specific for L-isomer
-
-
?
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
transfers the proS hydrogen at C-4 of the dihydropyridine ring of NAD(P)H to its substrate
-
-
-
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
Anabaena sp. PCC 7120
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
Streptococcus pyogenes ATCC 19615
-
-
-
-
?
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
Streptococcus pyogenes ATCC 19615
-
-
-
-
?
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-
-
-
-
r
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-, P32322
-
-
-
r
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-
activity assay, forward reaction
-
-
y
3,4-dehydro-DL-proline + NADPH
?
show the reaction diagram
-
-
-
-
?
3,4-dehydro-L-proline + NAD+
?
show the reaction diagram
-, P32322
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
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-Pro + NAD+
1-pyrroline-5-carboxylate + NADH
show the reaction diagram
-
-
-
-
-
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 + H+
show the reaction diagram
-
-
-
-
r
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
-
first step in proline metabolism the hepatocyte nuclear factors HNF4alpha and HNF1alpha regulate proline metabolism in adult liver
-
-
?
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
Q97ZT3, -
-
-
-
r
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
Q97ZT3, -
-
-
-
r
L-proline + NADP+
1-pyrroline-5-carboxylate + NADPH + H+
show the reaction diagram
-
-
-
-
r
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
Q97ZT3, -
-
-
-
r
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
-
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
final reaction of proline synthesis
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
ping pong mechanism
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
transfer of reducing equivalents from host plants to symbiotic partner
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
third enzyme in proline pathway, linkage to hexose monophosphate pathway
-
-
-
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
transfer of reducing equivalents into mitochondria, linkage to pentose phosphate pathway
-
-
?
L-thioproline + NAD(P)+
1-pyrroline-3-thio-5-carboxylate + NAD(P)H
show the reaction diagram
Q97ZT3, -
-
-
-
r
additional information
?
-
-
not: D-proline, L-hydroxyproline, L-azatidine-2-carboxylate, no other amino acids
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Streptococcus pyogenes, Streptococcus pyogenes ATCC 19615
-
-
-
-
?
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-
-
-
-
r
1-pyrroline-5-carboxylate + NADPH + H+
L-proline + NADP+
show the reaction diagram
-, P32322
-
-
-
r
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
-
-
-
-
r
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H + H+
show the reaction diagram
-
first step in proline metabolism the hepatocyte nuclear factors HNF4alpha and HNF1alpha regulate proline metabolism in adult liver
-
-
?
L-proline + NADP+
1-pyrroline-5-carboxylate + NADPH + H+
show the reaction diagram
-
-
-
-
r
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
-
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
final reaction of proline synthesis
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
discussion of role in vivo
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
ping pong mechanism
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
transfer of reducing equivalents from host plants to symbiotic partner
-
-
?
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
third enzyme in proline pathway, linkage to hexose monophosphate pathway
-
-
-
pyrroline-5-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
show the reaction diagram
-
transfer of reducing equivalents into mitochondria, linkage to pentose phosphate pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
Q97ZT3, -
2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM
NADH
-
preferentially
NADH
-
preferentially
NADH
-
preferred NADH over NADPH by a factor of at least 3fold
NADH
-
preferentially
NADH
-
preferentially
NADH
-
preferentially
NADH
-
preferentially
NADH
-
L-proline oxidation is strictly NAD+ dependent; preferentially
NADH
-
preferentially
NADH
-
with NADH the activity is markedly inhibited by physiological levels of NADP+, so NADH cannot serve as electron donor in vivo
NADP+
Q97ZT3, -
2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM
NADPH
-
preferentially
NADPH
-
preferred NADH over NADPH by a factor of at least 3fold
NADPH
-
no reaction
NADPH
-
preferentially
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ammonium acetate
-
increase of activity
KCl
-
increase of activity at 100 mM
KCl
-
2fold increase at 70 mM
Mg2+
-
increase of activity at 10 mM
Mg2+
-
activity is significantly increased in the forward reaction, optimal concentration of the cation is about 50-100 microM
Mg2+
P32322
-
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
-
increase of activity
potassium acetate
-
increase at 3 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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-carbamoylophenylaminomethylenebisphosphonic 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
-
-
-
Ag+
-
inactivation at 0.1 mM
Ag+
-
44% inactivation at 0.7 mM
Ag+
-
65% inactivation at 0.3 mM
ATP
-
competitive with respect to NADH, 50% inhibition at 0.1 mM
ATP
-
reversible with Mg2+
ATP
-
41% inactivation at 1 mM
ATP
-
70% inhibition at 2 mM
Cd2+
-
90% inhibition at 3.3 mM
CTP
-
91% inactivation at 1 mM reversible with Mg2+
Cu2+
-
90% inhibition at 3.3 mM
cysteine
-
77% inactivation at 10 mM
D-allohydroxyproline
-
competitive inhibition
GTP
-
100% inactivation at 10 mM, reversible with Mg2+
Hg2+
-
75% inactivation at 0.1 mM
Hg2+
-
65% inactivation at 0.3 mM
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
-
L-proline inhibits the inverse reaction at a concentration of 10-20 mM
N-ethylmaleimide
-
90% inhibition at 0.02 mM, inhibition can be prevented by NADH
NADH
-
above 0.16 mM
NADH
-
slight inhibition with 25% reduction of the catalytic rate at 200 mM
NADP+
-
43% inactivation at 1 mM
NADPH
-
above 0.13 mM
NaHSO3
-
88% inactivation at 1 mM
NH2OH
-
7% inactivation at 1 mM
NH2OH
-
92% inactivation at 1 mM
p-chloromercuribenzoate
-
complete inactivation at 1 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
complete inhibition at 0.125 mM, can be prevented by addition of dithiothreitol
p-chloromercuribenzoate
-
not
p-chloromercuribenzoate
-
not
p-hydroxymercuribenzoate
-
90% inhibition at 0.008 mM, inhibition can be prevented by addition of excess dithiothreitol
phosphate
-
-
proline
-
75% inactivation at 50 mM
proline
-
89% inhibition at 2 M
proline
-
39% inhibition of the NADH dependent activity and 17% of the NADPH dependent activity at 10 mM
proline
-
competitive inhibition
proline
-
12% inactivation at 50 mM
proline
-
-
proline
-
competitive inhibition
proline
-
competitive inhibitor of P5CR NAD(P)H-dependent thioproline dehydrogenase activity
proline
P32322
0.1 mM
pyrroline-5-carboxylate
-
substrate inhibition
Sodium bisulfite
-
-
stearoyl-CoA
-
competitive inhibitor of P5CR NAD(P)H-dependent thioproline dehydrogenase activity
thiazolidine-4-carboxylic acid
-
-
thiazolidine-4-carboxylic acid
-
-
thiazolidine-4-carboxylic acid
-
42% inhibition at 10 mM, L-isomer
thio-NAD+
-
65% inactivation at 0.2 mM
thio-NADP+
-
65% inactivation at 0.2 mM
Zn2+
-
14% inactivation at 1 mM
additional information
-
enzyme is not inhibited by the proline-analog L-thiazolidine-4-carboxylic acid
-
additional information
-
-
-
additional information
-
not inhibited by NADPH
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.04
-
1-pyrroline-5-carboxylate
-
cofactor NADH
0.047
-
1-pyrroline-5-carboxylate
-
cofactor NADPH
0.184
-
1-pyrroline-5-carboxylate
-
apparent value, with NADPH as cosubstrate, at pH 7.5 and 37C
0.349
-
1-pyrroline-5-carboxylate
-
apparent value, with NADH as cosubstrate, at pH 7.5 and 37C
0.141
-
3,4-dehydro-L-proline
P32322
-
4.4
-
DELTA1-pyrroline-3-hydroxy-5-carboxylate
-
-
0.051
-
DL-pyrroline-5-carboxylate
-
cosubstrate NADPH
0.08
-
DL-pyrroline-5-carboxylate
-
-
0.34
-
DL-pyrroline-5-carboxylate
-
-
0.62
-
DL-pyrroline-5-carboxylate
-
-
0.62
-
DL-pyrroline-5-carboxylate
-
cosubstrate NADH
1.25
-
L-proline
-
pH 10.2
1.55
-
L-proline
-
L-proline oxidation
31
-
L-proline
-
pH 8.0
0.021
-
L-pyrroline-5-carboxylate
-
cosubstrate NADPH
0.024
0.025
L-pyrroline-5-carboxylate
-
-
0.09
-
L-pyrroline-5-carboxylate
-
with NADH
0.09
-
L-pyrroline-5-carboxylate
-
-
0.12
-
L-pyrroline-5-carboxylate
-
with NADPH
0.12
-
L-pyrroline-5-carboxylate
-
with NADPH
0.125
-
L-pyrroline-5-carboxylate
-
-
0.14
-
L-pyrroline-5-carboxylate
-
with NADH
0.15
-
L-pyrroline-5-carboxylate
-
with NADPH
0.154
-
L-pyrroline-5-carboxylate
-
-
0.19
-
L-pyrroline-5-carboxylate
-
-
0.2
-
L-pyrroline-5-carboxylate
-
with NADH
0.21
0.3
L-pyrroline-5-carboxylate
-
NADH
0.21
-
L-pyrroline-5-carboxylate
-
cosubstrate NADH
0.33
-
L-pyrroline-5-carboxylate
-
pH 6.5; pH 8.0
0.37
-
L-pyrroline-5-carboxylate
-
with NADPH
0.44
-
L-pyrroline-5-carboxylate
-
-
0.45
-
L-pyrroline-5-carboxylate
-
with NADPH
0.53
-
L-pyrroline-5-carboxylate
-
with NADH
0.151
-
NAD+
-
wild type enzyme, 1 mM fixed thioproline, thioproline dehydrogenase activity assay
0.235
-
NAD+
-
E221A mutant, 1 mM fixed thioproline, thioproline dehydrogenase activity assay
10.5
-
NAD+
-
L-proline oxidation
0.1
-
NADH
-
-
0.176
-
NADH
-
apparent value, at pH 7.5 and 37C
0.19
-
NADH
-
chloroplast
0.2
-
NADH
-
-
0.23
-
NADH
-
-
0.43
-
NADH
-
etiolated shoots
1.55
-
NADH
-
-
0.48
-
NADP+
-
E221A mutant, 1 mM fixed thioproline, thioproline dehydrogenase activity assay
0.73
-
NADP+
-
E221A mutant, fixed 1 mM NADP+
1.26
-
NADP+
-
wild type enzyme, fixed 1 mM NADP+
3.06
-
NADP+
-
wild type enzyme, 1 mM fixed thioproline, thioproline dehydrogenase activity assay
0.006
-
NADPH
-
-
0.0071
-
NADPH
-
-
0.012
-
NADPH
-
apparent value, at pH 7.5 and 37C
0.03
-
NADPH
-
-
0.05
-
NADPH
-
-
0.06
-
NADPH
-
-
0.1
-
NADPH
-
etiolated shoots
0.12
-
NADPH
-
chloroplast
1.62
1.64
L-pyrroline-5-carboxylate
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00983
-
1-pyrroline-5-carboxylate
-
cofactor NADPH
387.3
-
1-pyrroline-5-carboxylate
-
cofactor NADH
451.7
-
1-pyrroline-5-carboxylate
-
cofactor NADPH
10
-
3,4-dehydro-L-proline
P32322
-
620
-
NADH
-
at pH 7.5 and 37C
13
-
NADP+
-
E221A mutant, fixed 1 mM NADP+
55
-
NADP+
-
wild type enzyme, fixed 1 mM NADP+
340
-
NADPH
-
at pH 7.5 and 37C
1270
-
pyrroline-5-carboxylate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
ATP
-
-
0.12
-
ATP
-
against DL-pyrroline-5-carboxylate
0.2
-
ATP
-
against NADH
0.0037
-
NADP+
-
against NADH
0.38
-
NADP+
-
against NADPH
0.32
-
ATP
-
against NADPH
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.187
-
2,3-dichlorophenylhydroxymethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.488
-
2-(2,3-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.431
-
2-(2,3-dichlorophenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
1.639
-
2-(2,6-dichlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.763
-
2-(2,6-dichlorophenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.463
-
2-(3,5-di(trifluoromethyl)phenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.082
-
2-(3,5-dichlorophenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
1.914
-
2-(3,5-dimethylphenyl)-1-hydroxyethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.386
-
2-(3,5-dimethylphenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.488
-
2-(4-benzylphenylamino)ethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
2.071
-
2-(4-chlorophenyl)-1-hydroxyethylidenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.413
-
3,5-di(trifluoromethyl)phenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.054
-
3,5-dibromophenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.719
-
3,5-difluorophenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
1.409
-
3,5-dimethylphenylhydroxymethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.547
-
3-carbamoylophenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
1.618
-
3-chlorophenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.852
-
4-benzylphenylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.325
-
4-benzylphenylhydroxymethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
0.684
-
5,6,7,8-tetrahydro-2-naphthylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
29
-
EDTA
-
at pH 7.5 and 37C
1.887
-
indan-5-ylaminomethylenebisphosphonic acid
-
in 100 mM HEPES-KOH buffer, pH 7.75, at 35C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.042
-
-
-
0.9
-
-
purification step supernatant, reverse reaction
1.6
-
P32322
purification step: soluble cell fraction
1.7
-
-
purification step supernatant, forward reaction
4.167
-
-
-
7.1
-
-
-
14
-
P32322
purification step: Ni-NTA agarose; purification step: Resource Q
21
-
P32322
purification step: ammonium sulfate precipitation
30
-
-
purification step Ni-NTA column, reverse reaction
32
-
P32322
purification step: Superdex 200
41.25
-
-
-
57
-
-
purification step Ni-NTA column, forward reaction
60
-
-
-
additional information
-
-
-
additional information
-
-
specific activity in different developmental stages of the embryo
additional information
-
-
subcellular distribution
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
various growth stages
additional information
-
-
-
additional information
-
-
specific activity in various mutant flies
additional information
-
-
assay method
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
cofactor NADH
6.05
-
-
-
6.5
-
-
in choroplasts
6.5
-
-
pyrroline-5-carboxylate reductase activity
6.7
7.4
-
-
6.8
7.5
-
pyrroline-5-carboxylate reductase activity
7
7.5
-
-
7
7.5
-
-
7
8
-
-
7
-
-
cofactor NADPH
7
-
Q97ZT3, -
reaction rate at pH 9.0 is nearly 3fold higher than at pH 7.0
7.2
-
-
activity assay
7.5
-
-
in etiolated shoots
7.5
-
-
activity assay, forward reaction
9
-
-
activity assay
9
-
P32322
activity assay
9
-
Q97ZT3, -
reaction rate is nearly 3fold higher than at pH 7.0
9.8
10.4
-
proline dehydrogenase activity
10
-
-
L-proline oxidation
10
-
-
L-proline dehydrogenase activity assay
10.2
-
-
proline dehydrogenase activity
10.3
-
-
activity assay, reverse reaction
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
-
pyrroline-5-carboxylate reductase activity
6
7
-
-
6
8.5
-
less than 50% of maximal activity above and below
8.5
-
-
no proline dehydrogenase activity below pH 8.5
9.2
10.5
-
proline dehydrogenase activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
activity assay
25
-
P32322
activity assay is performed at room temperature
37
-
-
assay at
37
-
-
activity assay
37
-
-
activity assay, forward and reverse reaction
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
DLD-1 colorectal cancer cell
Manually annotated by BRENDA team
-
colon adenocarcinoma cell
Manually annotated by BRENDA team
-
colorectal cancer cell, DLD-1 Tet-Off POX cells are generated for controlled expression of proline oxidase
Manually annotated by BRENDA team
P32322
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
-
from etiolated shoots
Manually annotated by BRENDA team
-
distribution in bovine cornea and lens
Manually annotated by BRENDA team
additional information
-
distribution in fetal and tumor tissues
Manually annotated by BRENDA team
additional information
-
distribution in different tissues
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
-
monomer, SDS-PAGE
30000
-
-
SDS-PAGE
30000
-
-
-
30000
-
-
SDS-PAGE
32000
-
-
SDS-PAGE
32000
-
-
after enterokinase treatment, estimated by 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
310000
-
-
-
320000
-
-
gel filtration
320000
-
Q97ZT3, -
gel filtration
365000
-
-
decamer, analysis of nondegenerated protein by native gel electrophoresis
370000
-
P32322
decamer, estimated by gel filtration and SDS-PAGE
additional information
-
-
up to 480000 kDa, quarternary structure changes drastically with buffer environment
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 28140, calculated from SDS-PAGE
?
Anabaena sp. PCC 7120
-
x * 28140, calculated from SDS-PAGE
-
decamer
-
10 * 28112, calculation from nucleotide sequence, SDS-PAGE
decamer
-
five homodimer subunits
decamer
-
10*32000-35600, estimated by SDS-PAGE, confirmed by spectrometric analysis
decamer
P32322
-
multimer
Q97ZT3, -
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes
multimer
-
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes
-
octamer
-
8 * 30000 SDS-PAGE; 8 * 30000, SDS-PAGE
octamer
-
8 * 25000 SDS-PAGE
polymer
-
12-16 * 30000 SDS-PAGE
polymer
-
10-12 * 28500
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P32322
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
Q97ZT3, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
irreversible inactivation below
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
complete inactivation after 30 min
0
-
-
30 min, loss of activity 16%-99%, highly dependent on buffer
22
-
-
96 h stable
37
-
-
4 h stable
60
-
-
10 min, complete inactivation
60
-
-
inactivation above
60
-
-
half life of the His-tagged protein is about 20 min
65
-
-
15 min stable
67
-
-
50% inactivation after 5 min
70
-
-
His-tagged protein is rapidly inactivated
70
-
Q97ZT3, -
stable for at least 30 min
80
-
Q97ZT3, -
half-life 30 min
90
-
P32322
irreversible loss of activity at 90C for 5 min
100
-
-
heating for 5 min completely destroys the enzyme
100
-
-
heating for 4 min completely destroys the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thiol reagents stabilize
-
sorbitol stabilizes
-
thiol reagents stabilize
-
sensitive to heat and low pH
-
dithiothreitol stabilizes during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, glutathione, EDTA
-
-20C, inactivation in few days, unstable in the absence of NADPH
-
-80C, 1 year
-
-18C, 0.15-0.2 M potassium phosphate buffer pH 7.4, 2 months
-
3C, 0.1 M sodium phosphate buffer pH 7.6, 10% (NH4)2SO4, 7 days
-
-10C, 50% loss of activity in 4 weeks
-
4C, 50% loss of activity in 1 weeks
-
-80C, 20 mM Caps, pH 9.4, 0.5 M NaCl, 6 months
P32322
-80C, 5% glycerol, 2 mM dithiothreitol, 1 month
-
-70C, 50 mM triethanolamine buffer pH 7.4, 9% w/v sucrose, 1 mM EDTA, 2 mM MgCl2, 30 mM 2-mercaptoethanol
-
-20C, 1 mg protein/ml, 50% glycerol, 0.1 mM dithiothreitol, unstable
-
-20C, 50% glycerol, 0.1 mM dithiothreitol, stable for 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni+2-NTA His-Trap resin column chromatography, and gel filtration
-
ammonium sulfate precipitation, anion exchange column chromatography, and gel filtration
-
copurification with proline oxidase, both activities located on the same protein
-
copurification with proline oxidase
-
copurification with thiazolidine-4-carboxylate dehydrogenase
-
homogeneity
-
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
P32322
homogeneity
-
by Ni-NTA His-binding resin affinity chromatography, the N-terminal fusion partner is cleaved by enterokinase
-
using a HiTrap Ni-NTA column
-
partial
-
2 isoenzymes
-
nickel affinity gel column chromatography
-
using a HiTrap Ni-NTA column
-
recombinant enzyme
Q97ZT3, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
fusion of enzyme promotor to beta-glucuronidase
-
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
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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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into a pET28a+ vector coding for a N-terminal His-tag for expression in Escherichia coli BL21DE3
P32322
proline oxidase cDNA is cloned into the pAdtrack vector, it is used to generate a recombinant adenovirus for transfection
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into the pET30a vector for expression in Escherichia coli BL21DE3
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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
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expressed in Escherichia coli BL21(DE3) pLysS cells
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
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oxidized low-density lipoproteins upregulate proline oxidase through nuclear receptor peroxisome proliferator-activated receptor gamma
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E221A
-
affinity for substrates is increased
E221G
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insoluble protein
additional information
-
N-truncation results in an insoluble protein, C-truncation does not alter the activity
additional information
A6NFM2
identification of a single homozygous region near the telomere of chromosome 17 in a cohort of patients with cutis laxa type 2. The single nucleotide change leads to a missense mutation adjacent to a slice junction in the gene encoding pyrroline-5-carboxylate reductase 1 which results in exon skipping and leads to deletion of reductase functional domain-coding region and an obligatory downstream frameshift
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
refolding after treatment with urea
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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overexpression of proline oxidase causes apoptotic cell death in a variety of cancer cells
medicine
-
mediating apoptosis in tumor cells
medicine
-
proline oxidase can mediate apoptosis through generation of reactive oxygen species
medicine
A6NFM2
identification of a single homozygous region near the telomere of chromosome 17 in a cohort of patients with cutis laxa type 2. The single nucleotide change leads to a missense mutation adjacent to a slice junction in the gene encoding pyrroline-5-carboxylate reductase 1 which results in exon skipping and leads to deletion of reductase functional domain-coding region and an obligatory downstream frameshift
medicine
-
micro-RNA miR-23b*, by targeting POX, may function as an oncogene. Pairs of human renal carcinoma and normal tissues show a negative correlation between miR-23b* and POX protein expression, providing its clinical corroboration. 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
medicine
-
pyrroline-5-carboxylate reductase is related to virulence of Mycobacterium tuberculosis