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Enzyme Nomenclature
Information on EC 1.5.1.52 - staphylopine dehydrogenase
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The expected taxonomic range for this enzyme is: Staphylococcus aureus
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EC NUMBER 
COMMENTARY 
1.5.1.52
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RECOMMENDED NAME
GeneOntology No.
staphylopine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
staphylopine + NADP+ + H2O = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + pyruvate + NADPH + H+
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
staphylopine:NADP+ oxidoreductase [(2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate]-forming
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
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
metabolism
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the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
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; the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
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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
physiological function
-
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
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; the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
? + NADP+ + H2O
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
? + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
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-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
? + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
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-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
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
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
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
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
A0A0H3JT80
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
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
A0A0H3JT80
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
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
-
the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.52)
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