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Literature summary extracted from

  • 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 (2016), Science, 352, 1105-1109 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.52 (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
-
?
1.5.1.52 (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

EC Number Organism UniProt Comment Textmining
1.5.1.52 Staphylococcus aureus A0A0H3JT80
-
-
1.5.1.52 Staphylococcus aureus ATCC 700699 A0A0H3JT80
-
-
2.5.1.152 Staphylococcus aureus A0A0H3JXA8
-
-
2.5.1.152 Staphylococcus aureus ATCC 700699 A0A0H3JXA8
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.52 (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
-
Staphylococcus aureus staphylopine + NADP+ + H2O
-
?
1.5.1.52 (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 Staphylococcus aureus staphylopine + NADP+ + H2O
-
?
1.5.1.52 (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + pyruvate + NADPH + H+
-
Staphylococcus aureus ATCC 700699 staphylopine + NADP+ + H2O
-
?
1.5.1.52 (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 Staphylococcus aureus ATCC 700699 staphylopine + NADP+ + H2O
-
?
2.5.1.152 S-adenosyl-L-methionine + D-histidine
-
Staphylococcus aureus N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.152 S-adenosyl-L-methionine + D-histidine
-
Staphylococcus aureus ATCC 700699 N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.52 cntM
-
Staphylococcus aureus
1.5.1.52 sav2468
-
Staphylococcus aureus
2.5.1.152 cntL
-
Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.52 NADPH the enzyme is specific for NADPH Staphylococcus aureus

General Information

EC Number General Information Comment Organism
1.5.1.52 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
1.5.1.52 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
2.5.1.152 physiological function the enzyme participates in the biosynthesis of the metallophore staphylopine. Staphylopine biosynthesis is impaired in the CntL mutant. The import of iron, zinc, nickel, and cobalt are all decreased in CntL mutants. CntL mutant strains are resistant to a concentration of cobalt that is toxic to the wild-type strain Staphylococcus aureus