Information on EC 1.5.1.21 - 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)

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

EC NUMBER
COMMENTARY hide
1.5.1.21
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RECOMMENDED NAME
GeneOntology No.
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-pipecolate + NADP+ = 1-piperideine-2-carboxylate + NADPH + H+
show the reaction diagram
(1)
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-
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L-proline + NADP+ = 1-pyrroline-2-carboxylate + NADPH + H+
show the reaction diagram
(2)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Lysine degradation
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Metabolic pathways
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Tropane, piperidine and pyridine alkaloid biosynthesis
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lysine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-pipecolate/L-proline:NADP+ 2-oxidoreductase
The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
52037-88-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC12633, gene dpkA
Uniprot
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-ketobutanoate + methylamine + NADPH
N-methyl-2-aminobutanoate + NADP+ + H2O
show the reaction diagram
10% of the rate with pyruvate
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-
?
alpha-ketohexanoate + methylamine + NADPH
N-methyl-2-aminohexanoate + NADP+ + H2O
show the reaction diagram
23% of the rate with pyruvate
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-
?
DELTA1-piperideine-2-carboxylate + NADH
L-pipecolate + NAD+
show the reaction diagram
DELTA1-piperideine-2-carboxylate + NADPH
L-pipecolate + NADP+
show the reaction diagram
DELTA1-pyrroline-2-carboxylate + NADPH
L-proline + NADP+
show the reaction diagram
fluoropyruvate + methylamine + NADPH
N-methylfluoroalanine + NADP+ + H2O
show the reaction diagram
14% of the rate with pyruvate
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?
phenylpyruvate + methylamine + NADPH
N-methylphenylalanine + NADP+ + H2O
show the reaction diagram
6.3% of the rate with pyruvate
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?
pyruvate + methylamine
N-methylalanine
show the reaction diagram
-
-
-
?
additional information
?
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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
DELTA1-piperideine-2-carboxylate + NADH
L-pipecolate + NAD+
show the reaction diagram
DELTA1-piperideine-2-carboxylate + NADPH
L-pipecolate + NADP+
show the reaction diagram
additional information
?
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Q5FB93
enzyme is involved in the catabolism of D-lysine and D-proline, pathway overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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slight inhibition
Co2+
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almost total inhibition at 0.1 mM
Hg2+
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almost total inhibition at 0.1 mM
KCN
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slight inhibition
Mg2+
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slight inhibition
Mn2+
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almost total inhibition at 0.1 mM
NADPH
p-chloromercuribenzoate
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almost total inhibition at 0.1 mM
pyrrole-2-carboxylate
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pyrroline-2-carboxylate
inhibits the reverse reaction
Zn2+
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almost total inhibition at 0.1 mM
additional information
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no effect: 0.1 mM L-cysteine, 0.1 mM iodoacetate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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slight activation at 1 mM
EDTA
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slight activation at 1 mM
Sodium diphosphate
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slight activation at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 1.6
DELTA1-piperideine-2-carboxylate
0.4
DELTA1-Pyrroline-5-carboxylate
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-
0.034 - 0.14
NADP+
0.034 - 0.14
NADPH
0.28
pyroglutamate
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-
additional information
additional information
kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
substrate and product inhibition kinetics, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.33
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADH
0.67
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADH
1.4
purified recombinant enzyme, substrates L-pipecolate and NADP+
51
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADPH
92
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADPH
140
substrate pyruvate, 30°C, pH 10.0
150
substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0
390
substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
assay at, forward reaction
10
assay at, reverse reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
2 * 36000, SDS-PAGE, crystallization data
200000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 36000, SDS-PAGE, crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unliganded form, in complex with NADPH, and with NADPH and pyrrole-2-carboxylate. subunit consists of domain I, NADPH-binding domain II, and domain III. Identification of catalytic Asp-Ser-His triad
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 35
stable for at least 30 min, pH 7.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol, 1 mM, protects during storage
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EDTA, 1 mM, protects during storage and against heat inactivation at 50°C
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NADP+, no protection during storage
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NADPH, protection during storage
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sodium diphosphate, 1 mM, protects during storage
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very unstable during purification
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, total loss of activity of the partially purified enzyme after 8 h, loss of activity can be prevented by adding low concentrations of EDTA, sodium diphosphate, dithiothreitol or L-pipecolic acid
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli, to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
dpk disruption mutant is unable to grow on D-lysine or D-proline as sole carbon source
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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enzymatic system for synthesis of L-pipecolic acid from L-lysine by commercial L-lysine alpha-oxidase and extract of Escherichia coli producing recombinant enzyme and glucose dehydrogenase. System provides 27g/l of L-pipecolic acid in laboratory scale, with 99.7% enantiomeric excess