BRENDA - Enzyme Database

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

Muramatsu, H.; Mihara, H.; Kakutani, R.; Yasuda, M.; Ueda, M.; Kurihara, T.; Esaki, N.; J. Biol. Chem. 280, 5329-5335 (2005)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.5.1.1
-
Pseudomonas putida
1.5.1.21
DNA sequence determination and analysis, overexpression in Escherichia coli
Pseudomonas putida
Engineering
EC Number
Protein Variants
Commentary
Organism
1.5.1.1
additional information
enzyme disruption mutant, strain is unable to use D-lysine or D-proline as a sole carbon source
Pseudomonas putida
1.5.1.21
additional information
dpk disruption mutant is unable to grow on D-lysine or D-proline as sole carbon source
Pseudomonas putida
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.21
NADPH
inhibits the reverse reaction
Pseudomonas putida
1.5.1.21
pyrroline-2-carboxylate
inhibits the reverse reaction
Pseudomonas putida
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.1.21
additional information
-
additional information
kinetics
Pseudomonas putida
1.5.1.21
0.034
-
NADP+
pH 10.0, 35°C, with substrate L-proline
Pseudomonas putida
1.5.1.21
0.034
-
NADPH
pH 8.0, 35°C, with substrate DELTA1-pyrroline-2-carboxylate
Pseudomonas putida
1.5.1.21
0.14
-
NADP+
pH 10.0, 35°C, with substrate L-pipecolate
Pseudomonas putida
1.5.1.21
0.14
-
NADPH
pH 8.0, 35°C, with substrate DELTA1-piperideine-2-carboxylate
Pseudomonas putida
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.5.1.1
additional information
Pseudomonas putida
involved in the catabolism of D-lysine and D-proline
?
-
-
-
1.5.1.21
additional information
Pseudomonas putida
enzyme is involved in the catabolism of D-lysine and D-proline, pathway overview
?
-
-
-
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.5.1.1
Pseudomonas putida
-
-
-
1.5.1.21
Pseudomonas putida
Q5FB93
strain ATCC12633, gene dpkA
-
1.5.1.21
Pseudomonas putida ATCC 12633
Q5FB93
strain ATCC12633, gene dpkA
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
1.5.1.21
recombinant enzyme from Escherichia coli, to homogeneity
Pseudomonas putida
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.1.21
additional information
specificity for carbon sources, wild-type shows the highest growth rate on D-proline, the deletion mutant on L-lysine, overview
Pseudomonas putida
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.5.1.1
0.33
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
0.67
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
1.4
-
oxidation of L-pipecolate, cosubstrate NADP+, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
5.4
-
oxidation of L-proline, cosubstrate NADP+, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
51
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
92
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.21
additional information
-
-
Pseudomonas putida
1.5.1.21
0.33
-
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADH
Pseudomonas putida
1.5.1.21
0.67
-
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADH
Pseudomonas putida
1.5.1.21
1.4
-
purified recombinant enzyme, substrates L-pipecolate and NADP+
Pseudomonas putida
1.5.1.21
51
-
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADPH
Pseudomonas putida
1.5.1.21
92
-
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADPH
Pseudomonas putida
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.5.1.1
DELTA1-piperidine-2-carboxylate + NAD(P)H
-
656290
Pseudomonas putida
L-pipecolic acid + NAD(P)+
-
-
-
r
1.5.1.1
DELTA1-pyrroline-2-carboxylate + NAD(P)H
at 55% of the rate with DELTA1-piperidine-2-carboxylate
656290
Pseudomonas putida
L-proline + NAD(P)+
-
-
-
r
1.5.1.1
L-pipecolic acid + NAD(P)+
at 26% of the rate with L-proline
656290
Pseudomonas putida
DELTA1-piperidine-2-carboxylate + NAD(P)H
-
-
-
r
1.5.1.1
L-proline + NAD(P)+
-
656290
Pseudomonas putida
DELTA1-pyrroline-2-carboxylate + NAD(P)H + H+
-
-
-
r
1.5.1.1
additional information
involved in the catabolism of D-lysine and D-proline
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.1
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
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.21
DELTA1-piperideine-2-carboxylate + NADPH
NADH is a poor electron donor, lower activity in the reverse reaction direction
656290
Pseudomonas putida
L-pipecolate + NADP+
-
-
-
r
1.5.1.21
DELTA1-pyrroline-2-carboxylate + NADPH
NADH is a poor electron donor, lower activity in the reverse reaction direction
656290
Pseudomonas putida
L-proline + NADP+
-
-
-
r
1.5.1.21
additional information
enzyme is involved in the catabolism of D-lysine and D-proline, pathway overview
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.21
additional information
substrate specificity, enzyme shows no malate or lactate dehydrogenase activity
656290
Pseudomonas putida
?
-
-
-
-
Synonyms
EC Number
Synonyms
Commentary
Organism
1.5.1.21
DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase
-
Pseudomonas putida
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.21
35
-
assay at
Pseudomonas putida
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.1.21
8
-
assay at, forward reaction
Pseudomonas putida
1.5.1.21
10
-
assay at, reverse reaction
Pseudomonas putida
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.1
NAD+
-
Pseudomonas putida
1.5.1.1
NADH
reaction with NADH is less than 1% of that with NADPH
Pseudomonas putida
1.5.1.1
NADP+
-
Pseudomonas putida
1.5.1.1
NADPH
reaction with NADH is less than 1% of that with NADPH
Pseudomonas putida
1.5.1.21
NADPH
dependent on
Pseudomonas putida
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.5.1.21
additional information
-
additional information
substrate and product inhibition kinetics, overview
Pseudomonas putida
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.5.1.1
-
Pseudomonas putida
1.5.1.21
DNA sequence determination and analysis, overexpression in Escherichia coli
Pseudomonas putida
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.1
NAD+
-
Pseudomonas putida
1.5.1.1
NADH
reaction with NADH is less than 1% of that with NADPH
Pseudomonas putida
1.5.1.1
NADP+
-
Pseudomonas putida
1.5.1.1
NADPH
reaction with NADH is less than 1% of that with NADPH
Pseudomonas putida
1.5.1.21
NADPH
dependent on
Pseudomonas putida
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
1.5.1.1
additional information
enzyme disruption mutant, strain is unable to use D-lysine or D-proline as a sole carbon source
Pseudomonas putida
1.5.1.21
additional information
dpk disruption mutant is unable to grow on D-lysine or D-proline as sole carbon source
Pseudomonas putida
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.21
NADPH
inhibits the reverse reaction
Pseudomonas putida
1.5.1.21
pyrroline-2-carboxylate
inhibits the reverse reaction
Pseudomonas putida
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.5.1.21
additional information
-
additional information
substrate and product inhibition kinetics, overview
Pseudomonas putida
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.1.21
additional information
-
additional information
kinetics
Pseudomonas putida
1.5.1.21
0.034
-
NADP+
pH 10.0, 35°C, with substrate L-proline
Pseudomonas putida
1.5.1.21
0.034
-
NADPH
pH 8.0, 35°C, with substrate DELTA1-pyrroline-2-carboxylate
Pseudomonas putida
1.5.1.21
0.14
-
NADP+
pH 10.0, 35°C, with substrate L-pipecolate
Pseudomonas putida
1.5.1.21
0.14
-
NADPH
pH 8.0, 35°C, with substrate DELTA1-piperideine-2-carboxylate
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.5.1.1
additional information
Pseudomonas putida
involved in the catabolism of D-lysine and D-proline
?
-
-
-
1.5.1.21
additional information
Pseudomonas putida
enzyme is involved in the catabolism of D-lysine and D-proline, pathway overview
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.5.1.21
recombinant enzyme from Escherichia coli, to homogeneity
Pseudomonas putida
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.1.21
additional information
specificity for carbon sources, wild-type shows the highest growth rate on D-proline, the deletion mutant on L-lysine, overview
Pseudomonas putida
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.5.1.1
0.33
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
0.67
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
1.4
-
oxidation of L-pipecolate, cosubstrate NADP+, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
5.4
-
oxidation of L-proline, cosubstrate NADP+, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
51
-
reduction of DELTA1-pyrroline-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.1
92
-
reduction of DELTA1-piperidine-2-carboxylate, cosubstrate NADPH, pH 8.0, 30°C
Pseudomonas putida
1.5.1.21
additional information
-
-
Pseudomonas putida
1.5.1.21
0.33
-
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADH
Pseudomonas putida
1.5.1.21
0.67
-
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADH
Pseudomonas putida
1.5.1.21
1.4
-
purified recombinant enzyme, substrates L-pipecolate and NADP+
Pseudomonas putida
1.5.1.21
51
-
purified recombinant enzyme, substrates DELTA1-pyrroline-2-carboxylate and NADPH
Pseudomonas putida
1.5.1.21
92
-
purified recombinant enzyme, substrates DELTA1-piperideine-2-carboxylate and NADPH
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.5.1.1
DELTA1-piperidine-2-carboxylate + NAD(P)H
-
656290
Pseudomonas putida
L-pipecolic acid + NAD(P)+
-
-
-
r
1.5.1.1
DELTA1-pyrroline-2-carboxylate + NAD(P)H
at 55% of the rate with DELTA1-piperidine-2-carboxylate
656290
Pseudomonas putida
L-proline + NAD(P)+
-
-
-
r
1.5.1.1
L-pipecolic acid + NAD(P)+
at 26% of the rate with L-proline
656290
Pseudomonas putida
DELTA1-piperidine-2-carboxylate + NAD(P)H
-
-
-
r
1.5.1.1
L-proline + NAD(P)+
-
656290
Pseudomonas putida
DELTA1-pyrroline-2-carboxylate + NAD(P)H + H+
-
-
-
r
1.5.1.1
additional information
involved in the catabolism of D-lysine and D-proline
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.1
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
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.21
DELTA1-piperideine-2-carboxylate + NADPH
NADH is a poor electron donor, lower activity in the reverse reaction direction
656290
Pseudomonas putida
L-pipecolate + NADP+
-
-
-
r
1.5.1.21
DELTA1-pyrroline-2-carboxylate + NADPH
NADH is a poor electron donor, lower activity in the reverse reaction direction
656290
Pseudomonas putida
L-proline + NADP+
-
-
-
r
1.5.1.21
additional information
enzyme is involved in the catabolism of D-lysine and D-proline, pathway overview
656290
Pseudomonas putida
?
-
-
-
-
1.5.1.21
additional information
substrate specificity, enzyme shows no malate or lactate dehydrogenase activity
656290
Pseudomonas putida
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.21
35
-
assay at
Pseudomonas putida
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.1.21
8
-
assay at, forward reaction
Pseudomonas putida
1.5.1.21
10
-
assay at, reverse reaction
Pseudomonas putida