Information on EC 1.5.1.52 - staphylopine dehydrogenase

for references in articles please use BRENDA:EC1.5.1.52
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The expected taxonomic range for this enzyme is: Staphylococcus aureus

EC NUMBER
COMMENTARY hide
1.5.1.52
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RECOMMENDED NAME
GeneOntology No.
staphylopine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
staphylopine + NADP+ + H2O = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + pyruvate + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
staphylopine biosynthesis
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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 hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
the enzyme is specific for NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
glyoxylate
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pH 8.0, 22°C
1.4
oxaloacetate
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pH 8.0, 22°C
0.029
pyruvate
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pH 8.0, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.074
glyoxylate
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pH 8.0, 22°C
0.26
NADPH
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pH 8.0, 22°C
0.26
oxaloacetate
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pH 8.0, 22°C
0.26
pyruvate
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pH 8.0, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
glyoxylate
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pH 8.0, 22°C
0.18
oxaloacetate
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pH 8.0, 22°C
8.9
pyruvate
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pH 8.0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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