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Information on EC 1.5.1.52 - staphylopine dehydrogenase
for references in articles please use BRENDA:EC1.5.1.52
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.52 staphylopine dehydrogenase
IUBMB Comments
The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
The expected taxonomic range for this enzyme is: Staphylococcus aureus
Reaction Schemes
showSynonyms
saodh, staphylopine dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cntM
SaODH
sav2468
staphylopine synthase
-
-
-
-
cntM
-
-
-
-
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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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SYSTEMATIC NAME
IUBMB Comments
staphylopine:NADP+ oxidoreductase [(2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate]-forming
The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+
? + NADP+ + H2O
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+
? + NADP+ + H2O
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: 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
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: 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
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: 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
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: the enzyme catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
Products: -
Products: -
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
staphylopine + NADP+ + H2O
Substrates: 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
Products: -
Products: -
?
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
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
metabolism
-
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
-
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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODH_STAAM
433
0
50072
Swiss-Prot
other Location (Reliability: 4)
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SUBUNIT
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McFarlane, J.S.; Davis, C.L.; Lamb, A.L.
Staphylopine, pseudopaline, and yersinopine dehydrogenases A structural and kinetic analysis of a new functional class of opine dehydrogenase
J. Biol. Chem.
293
8009-8019
2018
Staphylococcus aureus (A0A0H3JT80), Staphylococcus aureus ATCC 700699 (A0A0H3JT80)
brenda
Ghssein, G.; Brutesco, C.; Ouerdane, L.; Fojcik, C.; Izaute, A.; Wang, S.; Hajjar, C.; Lobinski, R.; Lemaire, D.; Richaud, P.; Voulhoux, R.; Espaillat, A.; Cava, F.; Pignol, D.; Borezee-Durant, E.; Arnoux, P.
Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus
Science
352
1105-1109
2016
Staphylococcus aureus (A0A0H3JT80), Staphylococcus aureus, Staphylococcus aureus ATCC 700699 (A0A0H3JT80)
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.1.52)
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Release 2026.1 (March 2026)
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