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Information on EC 1.5.1.1 - 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]
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1.5.1.1 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]IUBMB Comments
The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.
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Word Map
- 1.5.1.1
-
nadph-dependent
- cerebral
- dehydratase
- trans-3-hydroxy-l-proline
- d-lysine
- archaeon
- d-proline
- litoralis
-
extracerebral
-
forebrain
-
thermococcus
- saccharopine
-
ovine
- reductases
- collagen
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
pycr2, mu-crystallin, thyroid hormone binding protein, ketimine reductase, cytosolic thyroid hormone binding protein, pyr2c reductase, p2c reductase, p2c/pyr2c reductase, delta1-pyrroline-2-carboxylate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA1-Pyr2C reductase
DELTA1-pyrroline-2-carboxylate reductase
ketimine reductase
L-proline:NAD(P)+ 2-oxidoreductase
-
-
-
-
P2C reductase
P2C/Pyr2C reductase
Pyr2C reductase
pyrroline-2-carboxylate reductase
-
-
-
-
reductase, pyrroline-2-carboxylate
-
-
-
-
DELTA1-pyrroline-2-carboxylate reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+
(1)
-
-
-
L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+
(1) proposed catalytic mechanism of ketimine reductase
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Mobile domains I and II of protein change their conformations to produce the catalytic form. Preference for NADPH over NADH is explained by the cofactor binding site architecture
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
(2)
-
-
-
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
(2) proposed catalytic mechanism of ketimine reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-pipecolate/L-proline:NAD(P)+ 2-oxidoreductase
The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.
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CAS REGISTRY NUMBER
COMMENTARY
9029-16-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate + NADPH + H+
(4R)-4-hydroxy-L-proline + NADP+
-
-
-
r
1-pyrroline-(4R)-hydroxy-2-carboxylate + NADPH + H+
(4R)-hydroxy-L-proline + NADP+
-
-
-
r
cis-3-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
cis-4-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate + NADPH + H+
(4R)-hydroxy-L-proline + NADP+
-
-
-
r
L-pipecolate + NAD(P)+
1-piperideine-2-carboxylate + NAD(P)H + H+
-
-
-
r
L-pipecolic acid + NAD(P)+
DELTA1-piperidine-2-carboxylate + NAD(P)H
-
at 26% of the rate with L-proline
-
-
r
L-proline + NAD(P)+
1-pyrroline-2-carboxylate + NAD(P)H + H+
-
-
-
r
L-proline + NAD(P)+
DELTA1-pyrroline-2-carboxylate + NAD(P)H + H+
-
-
-
-
r
trans-4-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
-
-
-
r
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
-
-
-
-
r
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
-
-
-
r
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
Cercocebus sp.
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
r
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NADH + H+
L-pipecolate + NAD+
-
-
-
r
DELTA1-piperidine-2-carboxylate + NADH + H+
L-pipecolate + NAD+
-
-
-
r
DELTA1-piperidine-2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
r
DELTA1-piperidine-2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
ir
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
at 55% of the rate with DELTA1-piperidine-2-carboxylate
-
-
r
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
ir
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
ir
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
r
L-pipecolate + NAD+
DELTA1-piperidine-2-carboxylate + NADH + H+
-
-
-
r
L-pipecolate + NAD+
DELTA1-piperidine-2-carboxylate + NADH + H+
-
-
-
r
L-pipecolate + NADP+
DELTA1-piperidine-2-carboxylate + NADPH + H+
-
-
-
r
L-pipecolate + NADP+
DELTA1-piperidine-2-carboxylate + NADPH + H+
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
r
L-proline + NADP+
DELTA1-pyrroline-2-carboxylate + NADPH + H+
-
-
-
r
L-proline + NADP+
DELTA1-pyrroline-2-carboxylate + NADPH + H+
-
-
-
r
additional information
?
-
trans-3-hydroxy-L-proline is converted to proline by the purified LhpH and LhpI proteins, i.e. trans-3-hydroxy-L-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase, at pH 7.0. LhpI has dual metabolic functions as a reductase for DELTA1-pyrroline-2-carboxylate and DELTA1-piperidine-2-carboxylate
-
-
?
additional information
?
-
-
trans-3-hydroxy-L-proline is converted to proline by the purified LhpH and LhpI proteins, i.e. trans-3-hydroxy-L-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase, at pH 7.0. LhpI has dual metabolic functions as a reductase for DELTA1-pyrroline-2-carboxylate and DELTA1-piperidine-2-carboxylate
-
-
?
additional information
?
-
no activity with trans-4-hydroxy-D-proline, D-proline, trans-3-hydroxy-L-proline, cis-4-hydroxy-D-proline, and cis-3-hydroxy-D-proline, poor activity with trans-4-hydroxy-L-proline
-
-
?
additional information
?
-
-
no activity with trans-4-hydroxy-D-proline, D-proline, trans-3-hydroxy-L-proline, cis-4-hydroxy-D-proline, and cis-3-hydroxy-D-proline, poor activity with trans-4-hydroxy-L-proline
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
purified recombinant human CRYM possesses substantial KR activity. Ketimine reductase is a typical imine reductase. Substrate specificity of recombinant human ketimine reductase (KR) toward DELTA1-piperideine-2-carboxylate (P2CR) and various noncyclized imine intermediates, overview. N-methyl-L-alanine is produced when human KR is incubated in the presence of methylamine, NADPH and pyruvate. Human KR catalyzes the reductive alkylamination of phenylpyruvate and glyoxylate in the presence of methylamine. Substrate docking
-
-
-
additional information
?
-
-
purified recombinant human CRYM possesses substantial KR activity. Ketimine reductase is a typical imine reductase. Substrate specificity of recombinant human ketimine reductase (KR) toward DELTA1-piperideine-2-carboxylate (P2CR) and various noncyclized imine intermediates, overview. N-methyl-L-alanine is produced when human KR is incubated in the presence of methylamine, NADPH and pyruvate. Human KR catalyzes the reductive alkylamination of phenylpyruvate and glyoxylate in the presence of methylamine. Substrate docking
-
-
-
additional information
?
-
-
involved in the catabolism of D-lysine and D-proline
-
-
?
additional information
?
-
-
reverse reactions oxidizing L-proline or L-pipecolic acid are catalyzed at much lower rates. Very poor substrates: trans-4-hydroxy-L-proline, L-thioproline
-
-
?
additional information
?
-
-
the enzyme from kidney shows no activity with DELTA1-pyrroline-5-carboxylate and DELTA1-piperideine-6-carboxylate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
-
-
-
r
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
-
-
-
-
r
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
-
-
-
r
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
Cercocebus sp.
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
?
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
ir
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
-
-
-
-
ir
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
-
ir
additional information
?
-
trans-3-hydroxy-L-proline is converted to proline by the purified LhpH and LhpI proteins, i.e. trans-3-hydroxy-L-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase, at pH 7.0. LhpI has dual metabolic functions as a reductase for DELTA1-pyrroline-2-carboxylate and DELTA1-piperidine-2-carboxylate
-
-
?
additional information
?
-
-
trans-3-hydroxy-L-proline is converted to proline by the purified LhpH and LhpI proteins, i.e. trans-3-hydroxy-L-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase, at pH 7.0. LhpI has dual metabolic functions as a reductase for DELTA1-pyrroline-2-carboxylate and DELTA1-piperidine-2-carboxylate
-
-
?
additional information
?
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
-
reciprocal relationship between thyroid hormone binding and DELTA1-piperideine-2-carboxylate (P2C) binding to ketimine reductase
-
-
-
additional information
?
-
-
involved in the catabolism of D-lysine and D-proline
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
NADH and NADPH are equally effective as cofactor for the enzyme purified from rat kidney
-
additional information
-
the enzyme purified from porcine kidney shows equal activity with NADPH and NADH
-
additional information
the enzyme shows dual specificity for NADPH and NADH
-
additional information
-
the enzyme shows dual specificity for NADPH and NADH
-
additional information
the enzyme uses NADH and NADPH as reductant about equally well
-
additional information
-
the enzyme uses NADH and NADPH as reductant about equally well
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-formyl-L-methionine
-
non competitive inhibition, EDTA decreases the inhibition rate
additional information
the P2C reductase activity is potently inhibited by thyroid hormones
-
additional information
-
the P2C reductase activity is potently inhibited by thyroid hormones
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal Cancer Progression via Activating PI3K/AKT/mTOR Pathway.
African Swine Fever
African Swine Fever Virus Protein E199L Promotes Cell Autophagy through the Interaction of PYCR2.
Brain Diseases
Loss of PYCR2 Causes Neurodegeneration by Increasing Cerebral Glycine Levels via SHMT2.
Carcinogenesis
Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal Cancer Progression via Activating PI3K/AKT/mTOR Pathway.
Carcinoma, Hepatocellular
Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum.
Carcinoma, Hepatocellular
The upregulation of PYCR2 is associated with aggressive colon cancer progression and a poor prognosis.
Carcinoma, Squamous Cell
An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate.
Carcinoma, Squamous Cell
Characterization of a membrane-associated 3,3',5-triiodo-L-thyronine binding protein by use of monoclonal antibodies.
Choriocarcinoma
Regulation of thyroid hormone receptor-mediated transcription by a cytosol protein.
Colonic Neoplasms
The upregulation of PYCR2 is associated with aggressive colon cancer progression and a poor prognosis.
Deafness
CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea.
Deafness
Spiking Expression of mu-Crystallin mRNA during Treatment with Methimazole in Patients with Graves' Hyperthyroidism.
Hearing Loss
CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea.