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(4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate + NADPH + H+
(4R)-4-hydroxy-L-proline + NADP+
-
-
-
r
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
1-pyrroline-(4R)-hydroxy-2-carboxylate + NADPH + H+
(4R)-hydroxy-L-proline + NADP+
-
-
-
r
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
1-pyrroline-2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
?
cis-3-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
cis-4-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
DELTA1-piperideine 2-carboxylate + NADH + H+
L-pipecolate + NAD+
-
-
-
?
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 + NADH + H+
L-pipecolate + NAD+
DELTA1-piperidine-2-carboxylate + NADPH + H+
L-pipecolate + NADP+
DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate + NADPH + H+
(4R)-hydroxy-L-proline + NADP+
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADPH + H+
L-proline + NADP+
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
?
L-pipecolate + NAD(P)+
1-piperideine-2-carboxylate + NAD(P)H + H+
-
-
-
r
L-pipecolate + NAD+
DELTA1-piperidine-2-carboxylate + NADH + H+
L-pipecolate + NADP+
DELTA1-piperidine-2-carboxylate + NADPH + H+
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
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NADP+
DELTA1-pyrroline-2-carboxylate + NADPH + H+
trans-4-hydroxy-L-proline + NADP+
? + NADPH + H+
low activity
-
-
r
additional information
?
-
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-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
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
-
-
-
-
r
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
-
-
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
?
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
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)+
Cercocebus sp.
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
-
?
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)+
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-piperideine-2-carboxylate + NAD(P)H + H+
L-pipecolate + NAD(P)+
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + NAD(P)+
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
?
1-pyrroline-2-carboxylate + NADPH + H+
L-proline + NADP+
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADH + H+
L-pipecolate + NAD+
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH + H+
L-pipecolate + NADP+
DELTA1-piperidine-2-carboxylate + NAD(P)H
L-pipecolic acid + NAD(P)+
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
DELTA2-thiazoline-2-carboxylate + NADPH + H+
? + NADP+
-
-
-
?
additional information
?
-
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-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
1-pyrroline-2-carboxylate + NAD(P)H + H+
L-proline + 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)+
-
-
-
-
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)+
Cercocebus sp.
-
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
-
?
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)+
-
-
-
-
ir
DELTA1-pyrroline-2-carboxylate + NAD(P)H
L-proline + NAD(P)+
-
-
-
-
ir
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Cutis Laxa
Genetic analysis of Pycr1 and Pycr2 in mice.
Deafness
CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea.
Deafness
mu-crystallin, a NADPH-dependent T(3)-binding protein in cytosol.
Deafness
Spiking Expression of mu-Crystallin mRNA during Treatment with Methimazole in Patients with Graves' Hyperthyroidism.
Glioblastoma
Biomarker discovery: a proteomic approach for brain cancer profiling.
Hearing Loss
CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea.
Hepatitis
Thyroid hormone binding protein in chronic active hepatitis.
Hepatitis, Chronic
Thyroid hormone binding protein in chronic active hepatitis.
Hyperglycemia
Hyperglycemia induces elevated expression of thyroid hormone binding protein in vivo in kidney and heart and in vitro in mesangial cells.
Hyperglycemia
Loss of PYCR2 Causes Neurodegeneration by Increasing Cerebral Glycine Levels via SHMT2.
Hyperkinesis
PYCR2 Mutations cause a lethal syndrome of microcephaly and failure to thrive.
Hypersensitivity
PYCR1 and PYCR2 Interact and Collaborate with RRM2B to Protect Cells from Overt Oxidative Stress.
Hyperthyroidism
Concentration of serum thyroid hormone binding proteins after 131I treatment of hyperthyroidism.
Hyperthyroidism
Measurement of serum thyroxine binding prealbumin in various thyroidal states by radioimmunoassay.
Hyperthyroidism
Spiking Expression of mu-Crystallin mRNA during Treatment with Methimazole in Patients with Graves' Hyperthyroidism.
Hyperthyroidism
[Improved thyroid diagnosis in borderline hyperthyroidism by determination of free T3 index]
Infections
African Swine Fever Virus Protein E199L Promotes Cell Autophagy through the Interaction of PYCR2.
Kyphosis
Genetic analysis of Pycr1 and Pycr2 in mice.
Melanoma
Downregulation of pyrroline-5-carboxylate reductase-2 induces the autophagy of melanoma cells via AMPK/mTOR pathway.
Melanoma
The upregulation of PYCR2 is associated with aggressive colon cancer progression and a poor prognosis.
Microcephaly
Disease variants of human ?1-pyrroline-5-carboxylate reductase 2 (PYCR2).
Microcephaly
Expanding the genotypic spectrum of PYCR2 and a common ancestry in Thai patients with hypomyelinating leukodystrophy 10.
Microcephaly
Loss of PYCR2 Causes Neurodegeneration by Increasing Cerebral Glycine Levels via SHMT2.
Microcephaly
Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination.
Microcephaly
PYCR2 Mutation Causing Hypomyelination and Microcephaly in an Indian Child.
Microcephaly
PYCR2 Mutations cause a lethal syndrome of microcephaly and failure to thrive.
Movement Disorders
Expanding the genotypic spectrum of PYCR2 and a common ancestry in Thai patients with hypomyelinating leukodystrophy 10.
Muscle Hypotonia
PYCR2 Mutations cause a lethal syndrome of microcephaly and failure to thrive.
Muscular Diseases
Abnormal expression of mu-crystallin in facioscapulohumeral muscular dystrophy.
Muscular Dystrophies
Abnormal expression of mu-crystallin in facioscapulohumeral muscular dystrophy.
Muscular Dystrophy, Facioscapulohumeral
Abnormal expression of mu-crystallin in facioscapulohumeral muscular dystrophy.
Neoplasm Metastasis
Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal Cancer Progression via Activating PI3K/AKT/mTOR Pathway.
Neoplasm Metastasis
The upregulation of PYCR2 is associated with aggressive colon cancer progression and a poor prognosis.
Neoplasms
Moderate-Intensity Exercise Induces Neurogenesis and Improves Cognition in Old Mice by Upregulating Hippocampal Hippocalcin, Otub1, and Spectrin-?.
Neoplasms
Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal Cancer Progression via Activating PI3K/AKT/mTOR Pathway.
Neoplasms
The upregulation of PYCR2 is associated with aggressive colon cancer progression and a poor prognosis.
Paraplegia
Spastic paraplegia as the only symptom in two adult-onset patients carrying a novel pathogenic variant in PYCR2.
Spinal Cord Injuries
Comprehensive Corticospinal Labeling with mu-crystallin Transgene Reveals Axon Regeneration after Spinal Cord Trauma in ngr1-/- Mice.
Uterine Cervical Neoplasms
Identification of potential cervical cancer serum biomarkers in Thai patients.
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2.1
(4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.474 - 0.6
1-piperideine-2-carboxylate
0.491
1-pyrroline-(4R)-hydroxy-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
0.628 - 0.837
1-pyrroline-2-carboxylate
0.06 - 7.26
DELTA1-piperidine-2-carboxylate
0.491
DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.082 - 5.9
DELTA1-pyrroline-2-carboxylate
0.038
NADPH
-
+ DELTA1-pyrroline-2-carboxylate
0.474
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
0.6
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
0.628
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
0.837
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
0.06
DELTA1-piperidine-2-carboxylate
-
cosubstrate NADH
0.21
DELTA1-piperidine-2-carboxylate
-
-
0.474
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.6
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
7.26
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
7.26
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.082
DELTA1-pyrroline-2-carboxylate
-
cosubstrate NADH
0.12
DELTA1-pyrroline-2-carboxylate
-
cosubstrate NADPH
0.628
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.837
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
0.86
DELTA1-pyrroline-2-carboxylate
-
-
2.79
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
5.9
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
6.54
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
14.8
L-pipecolate
pH 10.5, 30°C, coenzyme: NAD+
80
L-pipecolate
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
80.1
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
3.63
L-proline
pH 10.5, 30°C, coenzyme: NADP+
3.99
L-proline
pH 10.5, 30°C, coenzyme: NAD+
18.3
L-proline
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
18.3
L-proline
pH 10.5, 30°C, coenzyme: NADP+
18.8
L-proline
purified recombinant His-tagged enzyme, with NAD+, pH 6.5, 30°C
18.8
L-proline
pH 10.5, 30°C, coenzyme: NAD+
0.02
NADH
-
+ DELTA1-piperidine-2-carboxylate
0.043
NADH
-
+ DELTA1-pyrroline-2-carboxylate
0.074
NADH
-
+ DELTA1-piperidine-2-carboxylate
0.43
NADH
-
+ DELTA1-pyrroline-2-carboxylate
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1.02
(4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
161.5 - 166
1-piperideine-2-carboxylate
10.35
1-pyrroline-(4R)-hydroxy-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
523 - 615
1-pyrroline-2-carboxylate
0.088 - 165.8
DELTA1-piperidine-2-carboxylate
10.35
DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
10.35 - 615
DELTA1-pyrroline-2-carboxylate
161.5
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
166
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
523
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
615
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
0.088
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
1.38
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
161.5
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
165.8
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
10.35
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
124.5
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
523.3
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
615
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
0.02
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
0.0213
L-pipecolate
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
2.5
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
3.7
L-pipecolate
pH 10.5, 30°C, coenzyme: NAD+
0.0069
L-proline
purified recombinant His-tagged enzyme, with NAD+, pH 6.5, 30°C
0.0069
L-proline
pH 10.5, 30°C, coenzyme: NAD+
1.09
L-proline
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
1.09
L-proline
pH 10.5, 30°C, coenzyme: NADP+
3.92
L-proline
pH 10.5, 30°C, coenzyme: NADP+
4.23
L-proline
pH 10.5, 30°C, coenzyme: NAD+
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0.124
(4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
269 - 350
1-piperideine-2-carboxylate
21.1
1-pyrroline-(4R)-hydroxy-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
735 - 833
1-pyrroline-2-carboxylate
0.0418 - 351.7
DELTA1-piperidine-2-carboxylate
21.2
DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
21.2 - 835
DELTA1-pyrroline-2-carboxylate
0.000027 - 0.38
L-pipecolate
269
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
350
1-piperideine-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
735
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C
833
1-pyrroline-2-carboxylate
purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C
0.0418
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
0.19
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
270
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
351.7
DELTA1-piperidine-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
21.2
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
225
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
735
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADH
835
DELTA1-pyrroline-2-carboxylate
pH 6.5, 30°C, coenzyme: NADPH
0.000027
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
0.00027
L-pipecolate
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
0.25
L-pipecolate
pH 10.5, 30°C, coenzyme: NAD+
0.38
L-pipecolate
pH 10.5, 30°C, coenzyme: NADP+
0.00037
L-proline
purified recombinant His-tagged enzyme, with NAD+, pH 6.5, 30°C
0.00037
L-proline
pH 10.5, 30°C, coenzyme: NAD+
0.0595
L-proline
pH 10.5, 30°C, coenzyme: NADP+
0.06
L-proline
purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C
1.06
L-proline
pH 10.5, 30°C, coenzyme: NAD+
1.08
L-proline
pH 10.5, 30°C, coenzyme: NADP+
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0.000457
substrates: L-pipecolate, NAD+, pH 10.5, 30°C
0.0005
purified recombinant His-tagged enzyme, substrates L-pipecolate and NAD+, pH 6.5, 30°C
0.00435
substrates: L-pipecolate, NADP+, pH 10.5, 30°C
0.0044
purified recombinant His-tagged enzyme, substrates L-pipecolate and NADP+, pH 6.5, 30°C
0.0045
purified recombinant His-tagged enzyme, substrates L-proline and NAD+, pH 6.5, 30°C
0.00451
substrates: L-proline, NAD+, pH 10.5, 30°C
0.0464
substrates: DELTA1-piperidine-2-carboxylate, NADH, pH 6.5, 30°C
0.174
substrates: (4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate, NADPH, pH 6.5, 30°C
0.291
substrates: DELTA1-piperidine-2-carboxylate, NADPH, pH 6.5, 30°C
0.33
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
0.67
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADH, pH 8.0, 30°C
1.4
-
oxidation of L-pipecolate, cosubstrate NADP+, pH 8.0, 30°C
2.72
substrates: L-pipecolate, NAD+, pH 10.5, 30°C
2.92
substrates: L-pipecolate, NADP+, pH 10.5, 30°C
30.2
substrates: DELTA1-pyrroline-2-carboxylate, NADPH, pH 6.5, 30°C
4.76
substrates: DELTA1-pyrroline-2-carboxylate, NADH, pH 6.5, 30°C
5.18
substrates: L-proline, NADP+, pH 10.5, 30°C
5.4
-
oxidation of L-proline, cosubstrate NADP+, pH 8.0, 30°C
5.5
substrates: L-proline, NAD+, pH 10.5, 30°C
51
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
92
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
0.63
purified recombinant His-tagged enzyme, substrates L-proline and NADP+, pH 6.5, 30°C
0.63
substrates: L-proline, NADP+, pH 10.5, 30°C
12
purified recombinant His-tagged enzyme, substrates 1-pyrroline-(4R)-hydroxy-2-carboxylate and NADH, pH 6.5, 30°C
12
substrates: DELTA1-pyrroline-(4R)-hydroxy-2-carboxylate, NADPH, pH 6.5, 30°C
177
purified recombinant His-tagged enzyme, substrates 1-piperideine-2-carboxylate and NADH, pH 6.5, 30°C
177
substrates: DELTA1-piperidine-2-carboxylate, NADH, pH 6.5, 30°C
220
purified recombinant His-tagged enzyme, substrates 1-piperideine-2-carboxylate and NADPH, pH 6.5, 30°C
220
substrates: DELTA1-piperidine-2-carboxylate, NADPH, pH 6.5, 30°C
584
purified recombinant His-tagged enzyme, substrates 1-pyrroline-2-carboxylate and NADPH, pH 6.5, 30°C
584
substrates: DELTA1-pyrroline-2-carboxylate, NADPH, pH 6.5, 30°C
600
purified recombinant His-tagged enzyme, substrates 1-pyrroline-2-carboxylate and NADH, pH 6.5, 30°C
600
substrates: DELTA1-pyrroline-2-carboxylate, NADH, pH 6.5, 30°C
additional information
-
specific activities in various brain regions
additional information
Cercocebus sp.
-
specific activities in various brain regions
additional information
-
specific activities in various brain regions
additional information
-
specific activities in homogenates of various organs
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evolution
enzyme Pyr2C reductase is a member of the ornithine cyclodeaminase/micro-crystallin superfamily, different from known dpkA protein, and there are several significant differences in the enzymatic properties between Azospirillum brasilense and another bacteria: substrate and coenzyme specificities, phylogenetic analysis
evolution
enzymes that reduce DELTA1-pyrroline-5-carboxylate and DELTA1-piperideine-6-carboxylate are aldimine reductases whereas enzymes that reduce DELTA1-piperideine-2-carboxylate and DELTA1-pyrroline-2-carboxylate (P2C/Pyr2C) are ketimine reductases (KRs)
malfunction
disruption of LhpI gene from Azospirillum brasilense leads to loss of growth on trans-3-hydroxy-L-proline (T3LHyp), D-proline and D-lysine
malfunction
disruption of LhpI gene from Azospirillum brasilense leads to loss of growth on trans-3-hydroxy-L-proline, D-proline and D-lysine, indicating that this gene has dual metabolic functions as a reductase for Pyr2C and DELTA1-piperidine-2-carboxylate in these pathways, and that the T3LHyp pathway is not linked to trans-4-hydroxy-L-proline and L-proline metabolism
metabolism
the enzyme is involved in the trans-3-hydroxy-L-proline pathway and the metabolic networks with D-lysine and D-proline, overview. The trans-3-hydroxy-L-proline pathway is not linked to trans-4-hydroxy-L-proline and L-proline metabolism
metabolism
lysine degradation may be divided into two distinct pathways, namely (1) the pipecolate pathway which involves oxidation at the alpha-amino position followed by reduction of the product (P2C) to pipecolate by ketimine reductase (KR), and (2) the saccharopine pathway which involves oxidation at the epsilon-amino position The saccharopine pathway is predominantly mitochondrial, whereas the pipecolate pathway is predominantly cytosolic (but with a portion occurring in the peroxisomes). The DELTA1-piperideine-2-carboxylate (P2C) reductase enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Unique presence of the pipecolate pathway in brain. Cerebral pipecolate pathway, overview
physiological function
enzyme AbLhpI is a bifunctional NAD(P)H-dependent Delta1-pyrroline-2-carboxylate/Delta1-piperideine-2-carboxylate reductase (Pyr2C/Pip2C reductase)
physiological function
-
the enzymatic reduction of Pyr2C to L-proline together with DAAO may be regarded as a salvage mechanism for converting D-proline, arising from the diet or intestinal bacteria, to L-proline, the more biological useful enantiomer in mammals
physiological function
identification of ketimine reductase (KR) as mu-crystalin (CRYM)/cytosolic thyroid hormone binding protein (THBP). CRYM is a major mammalian THBP, which has the ability to strongly bind thyroid hormones in an NADPH-dependent fashion. It is also active as a DELTA1-piperideine-2-carboxylate (P2C) reductase, which catalyzes the NAD(P)H-dependent reduction of -C=N- (imine) double bonds of a number of cyclic ketimine substrates including sulfur-containing cyclic ketimines. P2C exists in equilibrium with its open-chain form under acidic conditions, but at neutral pH, P2C exists predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form). P2C can also exist as an enamine, but only at basic pH values. The enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Although KR is important in the formation of L-pipecolate in the brain, it is also an important source of L-proline. This proline (via proline oxidase) in turn is an important source of DELTA1-pyrroline-5-carboxylate (Pyr5C) and hence of glutamate and to a lesser extent ornithine. Ketimine reductase is involved in several diseases
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Garweg, G.; von Rehren, D.; Hintze, U.
L-Pipecolate formation in the mammalian brain. Regional distribution of DELTA1-pyrroline-2-carboxylate reductase activity
J. Neurochem.
35
616-621
1980
Canis lupus familiaris, Cercocebus sp., Mus musculus
brenda
Meister, A.; Radhakrishnan, A.N.; Buckley, S.D.
Enzymatic synthesis of L-pipecolic acid and L-proline
J. Biol. Chem.
229
789-800
1957
Klebsiella aerogenes, Neurospora crassa, Vigna radiata var. radiata, Pisum sativum, Rattus norvegicus
brenda
Muramatsu, H.; Mihara, H.; Kakutani, R.; Yasuda, M.; Ueda, M.; Kurihara, T.; Esaki, N.
The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline
J. Biol. Chem.
280
5329-5335
2005
Pseudomonas putida
brenda
Goto, M.; Muramatsu, H.; Mihara, H.; Kurihara, T.; Esaki, N.; Omi, R.; Miyahara, I.; Hirotsu, K.
Crystal structures of DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction
J. Biol. Chem.
280
40875-40884
2005
Pseudomonas syringae (Q4U331)
brenda
Hallen, A.; Jamie, J.F.; Cooper, A.J.
Lysine metabolism in mammalian brain an update on the importance of recent discoveries
Amino Acids
45
1249-1272
2013
Rattus norvegicus, Sus scrofa
brenda
Watanabe, S.; Tanimoto, Y.; Yamauchi, S.; Tozawa, Y.; Sawayama, S.; Watanabe, Y.
Identification and characterization of trans-3-hydroxy-l-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria
FEBS Open Bio
4
240-250
2014
Colwellia psychrerythraea (Q485R8), Azospirillum brasilense (V5YW53), Azospirillum brasilense
brenda
Hallen, A.; Jamie, J.; Cooper, A.
Imine reductases A comparison of glutamate dehydrogenase to ketimine reductases in the brain
Neurochem. Res.
39
527-541
2014
Rattus norvegicus
-
brenda
Hallen, A.; Cooper, A.J.
Reciprocal control of thyroid binding and the pipecolate pathway in the brain
Neurochem. Res.
42
217-243
2017
Homo sapiens (Q14894), Homo sapiens
brenda