BRENDA - Enzyme Database
show all sequences of 1.5.1.21

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)
Crystallization (Commentary)
Organism
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
Inhibitors
Commentary
Organism
Structure
2-picolinate
-
Pseudomonas syringae
pyrrole-2-carboxylate
-
Pseudomonas syringae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas syringae
Q4U331
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
140
-
substrate pyruvate, 30°C, pH 10.0
Pseudomonas syringae
150
-
substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
390
-
substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
alpha-ketobutanoate + methylamine + NADPH
10% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminobutanoate + NADP+ + H2O
-
-
-
?
alpha-ketohexanoate + methylamine + NADPH
23% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminohexanoate + NADP+ + H2O
-
-
-
?
DELTA1-piperideine-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-pipecolate + NADP+
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-proline + NADP+
-
-
-
?
fluoropyruvate + methylamine + NADPH
14% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylfluoroalanine + NADP+ + H2O
-
-
-
?
additional information
no substrate: alpha-ketovalerate, ammonia
674509
Pseudomonas syringae
?
-
-
-
-
phenylpyruvate + methylamine + NADPH
6.3% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylphenylalanine + NADP+ + H2O
-
-
-
?
pyruvate + methylamine
-
674509
Pseudomonas syringae
N-methylalanine
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Synonyms
Synonyms
Commentary
Organism
DpkA
-
Pseudomonas syringae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
45
-
Pseudomonas syringae
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
35
stable for at least 30 min, pH 7.0
Pseudomonas syringae
Cofactor
Cofactor
Commentary
Organism
Structure
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
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)
Cofactor
Commentary
Organism
Structure
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
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)
Crystallization
Organism
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)
Inhibitors
Commentary
Organism
Structure
2-picolinate
-
Pseudomonas syringae
pyrrole-2-carboxylate
-
Pseudomonas syringae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
140
-
substrate pyruvate, 30°C, pH 10.0
Pseudomonas syringae
150
-
substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
390
-
substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0
Pseudomonas syringae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
alpha-ketobutanoate + methylamine + NADPH
10% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminobutanoate + NADP+ + H2O
-
-
-
?
alpha-ketohexanoate + methylamine + NADPH
23% of the rate with pyruvate
674509
Pseudomonas syringae
N-methyl-2-aminohexanoate + NADP+ + H2O
-
-
-
?
DELTA1-piperideine-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-pipecolate + NADP+
-
-
-
?
DELTA1-pyrroline-2-carboxylate + NADPH
-
674509
Pseudomonas syringae
L-proline + NADP+
-
-
-
?
fluoropyruvate + methylamine + NADPH
14% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylfluoroalanine + NADP+ + H2O
-
-
-
?
additional information
no substrate: alpha-ketovalerate, ammonia
674509
Pseudomonas syringae
?
-
-
-
-
phenylpyruvate + methylamine + NADPH
6.3% of the rate with pyruvate
674509
Pseudomonas syringae
N-methylphenylalanine + NADP+ + H2O
-
-
-
?
pyruvate + methylamine
-
674509
Pseudomonas syringae
N-methylalanine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 36000, SDS-PAGE, crystallization data
Pseudomonas syringae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
45
-
Pseudomonas syringae
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
35
stable for at least 30 min, pH 7.0
Pseudomonas syringae
Other publictions for EC 1.5.1.21
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743355
Hallen
Reciprocal control of thyroid ...
Canis lupus familiaris, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa
Neurochem. Res.
42
217-243
2017
-
-
-
-
-
-
6
-
6
-
-
13
-
6
-
-
-
-
-
20
-
-
19
-
18
-
-
-
-
-
-
-
8
-
-
-
-
-
-
8
-
-
-
-
6
-
-
6
-
-
13
-
-
-
-
-
20
-
-
19
-
-
-
-
-
-
-
-
-
-
18
18
-
-
-
742531
Watanabe
Identification and characteri ...
Pseudomonas aeruginosa
FEBS Open Bio
4
240-250
2014
-
-
1
-
-
-
-
6
-
-
1
4
-
1
-
-
-
-
-
1
5
-
12
1
6
1
-
-
6
2
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
6
-
-
1
4
-
-
-
-
-
1
5
-
12
1
1
-
-
6
2
-
-
-
-
2
2
-
6
6
741580
Hallen
Lysine metabolism in mammalia ...
Bos taurus, Mus musculus, Rattus norvegicus, Sus scrofa
Amino Acids
45
1249-1272
2013
-
-
-
-
-
-
-
-
8
-
2
8
-
4
-
-
2
-
-
5
-
-
8
1
12
-
-
-
-
5
-
-
6
-
-
-
-
-
-
6
-
-
-
-
-
-
-
8
-
2
8
-
-
-
2
-
5
-
-
8
1
-
-
-
-
5
-
-
-
-
-
-
-
-
-
724927
Umair
Lysine catabolism in Haemonchu ...
Haemonchus contortus, Teladorsagia circumcincta
Exp. Parasitol.
131
101-106
2012
-
-
-
-
-
-
-
2
-
-
-
4
-
4
-
-
-
-
-
4
-
-
4
-
4
-
-
-
-
2
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
2
-
-
-
4
-
-
-
-
-
4
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
672675
Muramatsu
Enzymatic synthesis of L-pipec ...
Pseudomonas putida
Biosci. Biotechnol. Biochem.
70
2296-2298
2006
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656290
Muramatsu
The putative malate/lactate de ...
Pseudomonas putida, Pseudomonas putida ATCC 12633
J. Biol. Chem.
280
5329-5335
2005
-
-
1
-
1
-
2
5
-
-
-
1
-
5
-
-
1
-
-
1
6
-
4
-
1
1
-
-
-
2
-
-
1
1
-
-
-
-
1
1
-
1
-
-
2
1
5
-
-
-
1
-
-
-
1
-
1
6
-
4
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
674509
Goto
Crystal structures of DELTA1-p ...
Pseudomonas syringae
J. Biol. Chem.
280
40875-40884
2005
-
-
-
1
-
-
2
-
-
-
1
-
-
2
-
-
-
-
-
-
3
-
8
1
1
1
-
1
-
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
3
-
8
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
392171
Cao
The OCT plasmid encodes D-lysi ...
Pseudomonas putida
Plasmid
30
83-89
1993
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392169
Payton
DELTA1-Piperideine-2-carboxyla ...
Pseudomonas putida
J. Bacteriol.
149
864-871
1982
3
-
-
-
-
6
11
4
-
-
1
1
-
2
-
-
1
-
-
-
1
1
3
-
-
1
-
-
-
1
-
-
2
-
-
-
3
-
-
2
-
-
6
-
11
-
4
-
-
1
1
-
-
-
1
-
-
1
1
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
2133
Chang
D-lysine catabolic pathway in ...
Pseudomonas putida
J. Bacteriol.
117
753-764
1974
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-