BRENDA - Enzyme Database
show all sequences of 1.5.1.52

Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus

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.; Science 352, 1105-1109 (2016)

Data extracted from this reference:

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, which is involved in the acquisition of nickel, copper, and cobalt
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, which is involved in the acquisition of nickel, copper, and cobalt
staphylopine + NADP+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
A0A0H3JT80
-
-
Staphylococcus aureus ATCC 700699
A0A0H3JT80
-
-
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 + pyruvate + NADPH + H+
-
749374
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, which is involved in the acquisition of nickel, copper, and cobalt
749374
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
-
749374
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 catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
749374
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme is specific for NADPH
Staphylococcus aureus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme is specific for NADPH
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, which is involved in the acquisition of nickel, copper, and cobalt
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, which is involved in the acquisition of nickel, copper, and cobalt
staphylopine + NADP+ + H2O
-
-
?
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 + pyruvate + NADPH + H+
-
749374
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, which is involved in the acquisition of nickel, copper, and cobalt
749374
Staphylococcus aureus
staphylopine + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
-
749374
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 catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt
749374
Staphylococcus aureus ATCC 700699
staphylopine + NADP+ + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
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
Staphylococcus aureus
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
Staphylococcus aureus
General Information (protein specific)
General Information
Commentary
Organism
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
Staphylococcus aureus
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
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
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1
1
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3
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2
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3
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1
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8
1
1
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4
1
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1
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1
1
1
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3
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2
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1
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8
1
1
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4
1
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2
2
-
3
3
749374
Ghssein
Biosynthesis of a broad-spect ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699
Science
352
1105-1109
2016
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2
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5
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4
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1
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-
1
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2
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4
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2
2
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