BRENDA - Enzyme Database
show all sequences of 1.5.1.52

Staphylopine, pseudopaline, and yersinopine dehydrogenases A structural and kinetic analysis of a new functional class of opine dehydrogenase

McFarlane, J.S.; Davis, C.L.; Lamb, A.L.; J. Biol. Chem. 293, 8009-8019 (2018)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Staphylococcus aureus
Crystallization (Commentary)
Crystallization
Organism
crystals are grown in hanging drops composed of 0.0015 ml of protein and 0.0015 ml of well solution at 24°C. The crystals are transferred into well solution supplemented with 25% glycerol as a cryoprotectant and flash-cooled in liquid nitrogen prior to data collection
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.029
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
1.4
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
3
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
Staphylococcus aureus
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
staphylopine + NADP+ + H2O
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
Staphylococcus aureus ATCC 700699
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
staphylopine + NADP+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
A0A0H3JT80
-
-
Staphylococcus aureus ATCC 700699
A0A0H3JT80
-
-
Purification (Commentary)
Commentary
Organism
-
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
748236
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
748236
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
-
Staphylococcus aureus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Staphylococcus aureus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.074
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
NADPH
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Staphylococcus aureus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme is specific for NADPH
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Staphylococcus aureus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme is specific for NADPH
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystals are grown in hanging drops composed of 0.0015 ml of protein and 0.0015 ml of well solution at 24°C. The crystals are transferred into well solution supplemented with 25% glycerol as a cryoprotectant and flash-cooled in liquid nitrogen prior to data collection
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.029
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
1.4
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
3
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
Staphylococcus aureus
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
staphylopine + NADP+ + H2O
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
Staphylococcus aureus ATCC 700699
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
staphylopine + NADP+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
? + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
748236
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
748236
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
748236
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Staphylococcus aureus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Staphylococcus aureus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.074
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
NADPH
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
0.26
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Staphylococcus aureus
General Information
General Information
Commentary
Organism
metabolism
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
Staphylococcus aureus
physiological function
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
Staphylococcus aureus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
Staphylococcus aureus
physiological function
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine. The metallophore play an important role in metal acquisition of zinc, cobalt, nickel, and iron and is also associated with the pathogenesis of several disease states
Staphylococcus aureus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
0.18
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
8.9
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
glyoxylate
pH 8.0, 22°C
Staphylococcus aureus
0.18
-
oxaloacetate
pH 8.0, 22°C
Staphylococcus aureus
8.9
-
pyruvate
pH 8.0, 22°C
Staphylococcus aureus
Other publictions for EC 1.5.1.52
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
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)
748236
McFarlane
Staphylopine, pseudopaline, a ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699
J. Biol. Chem.
293
8009-8019
2018
-
-
1
1
-
-
-
3
-
-
-
2
-
3
-
-
1
-
-
-
-
-
8
1
1
-
-
4
1
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
3
-
-
-
2
-
-
-
1
-
-
-
-
8
1
1
-
-
4
1
-
-
-
-
2
2
-
3
3
749374
Ghssein
Biosynthesis of a broad-spect ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699
Science
352
1105-1109
2016
-
-
-
-
-
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-