BRENDA - Enzyme Database

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

Goto, M.; Muramatsu, H.; Mihara, H.; Kurihara, T.; Esaki, N.; Omi, R.; Miyahara, I.; Hirotsu, K.; J. Biol. Chem. 280, 40875-40884 (2005)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization (Commentary)
Organism
1.5.1.1
unliganded enzyme, in complex with NADPH, and in complex with NADPH and pyrrole-2-carboxylate
Pseudomonas syringae
1.5.1.21
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
Pseudomonas syringae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.21
2-picolinate
-
Pseudomonas syringae
1.5.1.21
pyrrole-2-carboxylate
-
Pseudomonas syringae
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.5.1.21
36000
-
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.5.1.1
Pseudomonas syringae
Q4U331
-
-
1.5.1.21
Pseudomonas syringae
Q4U331
-
-
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
1.5.1.1
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
Pseudomonas syringae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.5.1.21
140
-
substrate pyruvate, 30°C, pH 10.0
Pseudomonas syringae
1.5.1.21
150
-
substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
1.5.1.21
390
-
substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.5.1.21
alpha-ketobutanoate + methylamine + NADPH
10% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminobutanoate + NADP+ + H2O
-
-
-
?
1.5.1.21
alpha-ketohexanoate + methylamine + NADPH
23% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminohexanoate + NADP+ + H2O
-
-
-
?
1.5.1.21
DELTA1-piperideine-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-pipecolate + NADP+
-
-
-
?
1.5.1.21
DELTA1-pyrroline-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-proline + NADP+
-
-
-
?
1.5.1.21
fluoropyruvate + methylamine + NADPH
14% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylfluoroalanine + NADP+ + H2O
-
-
-
?
1.5.1.21
additional information
no substrate: alpha-ketovalerate, ammonia
674509
Pseudomonas syringae
?
-
-
-
-
1.5.1.21
phenylpyruvate + methylamine + NADPH
6.3% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylphenylalanine + NADP+ + H2O
-
-
-
?
1.5.1.21
pyruvate + methylamine
-
674509
Pseudomonas syringae
N-methylalanine
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.5.1.1
dimer
crystallization data
Pseudomonas syringae
1.5.1.21
dimer
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Synonyms
EC Number
Synonyms
Commentary
Organism
1.5.1.21
DpkA
-
Pseudomonas syringae
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.21
30
45
-
Pseudomonas syringae
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.5.1.21
-
35
stable for at least 30 min, pH 7.0
Pseudomonas syringae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.1
NADP+
preference for NADPH over NADH
Pseudomonas syringae
1.5.1.1
NADPH
preference for NADPH over NADH
Pseudomonas syringae
1.5.1.21
NADH
specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture
Pseudomonas syringae
1.5.1.21
NADPH
specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture
Pseudomonas syringae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.5.1.1
NADP+
preference for NADPH over NADH
Pseudomonas syringae
1.5.1.1
NADPH
preference for NADPH over NADH
Pseudomonas syringae
1.5.1.21
NADH
specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture
Pseudomonas syringae
1.5.1.21
NADPH
specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture
Pseudomonas syringae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.5.1.1
unliganded enzyme, in complex with NADPH, and in complex with NADPH and pyrrole-2-carboxylate
Pseudomonas syringae
1.5.1.21
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
Pseudomonas syringae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.5.1.21
2-picolinate
-
Pseudomonas syringae
1.5.1.21
pyrrole-2-carboxylate
-
Pseudomonas syringae
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.5.1.21
36000
-
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.5.1.21
140
-
substrate pyruvate, 30°C, pH 10.0
Pseudomonas syringae
1.5.1.21
150
-
substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
1.5.1.21
390
-
substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.5.1.21
alpha-ketobutanoate + methylamine + NADPH
10% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminobutanoate + NADP+ + H2O
-
-
-
?
1.5.1.21
alpha-ketohexanoate + methylamine + NADPH
23% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminohexanoate + NADP+ + H2O
-
-
-
?
1.5.1.21
DELTA1-piperideine-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-pipecolate + NADP+
-
-
-
?
1.5.1.21
DELTA1-pyrroline-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-proline + NADP+
-
-
-
?
1.5.1.21
fluoropyruvate + methylamine + NADPH
14% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylfluoroalanine + NADP+ + H2O
-
-
-
?
1.5.1.21
additional information
no substrate: alpha-ketovalerate, ammonia
674509
Pseudomonas syringae
?
-
-
-
-
1.5.1.21
phenylpyruvate + methylamine + NADPH
6.3% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylphenylalanine + NADP+ + H2O
-
-
-
?
1.5.1.21
pyruvate + methylamine
-
674509
Pseudomonas syringae
N-methylalanine
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.5.1.1
dimer
crystallization data
Pseudomonas syringae
1.5.1.21
dimer
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.1.21
30
45
-
Pseudomonas syringae
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.5.1.21
-
35
stable for at least 30 min, pH 7.0
Pseudomonas syringae