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Literature summary extracted from

  • McFarlane, J.S.; Lamb, A.L.
    Biosynthesis of an opine metallophore by Pseudomonas aeruginosa (2017), Biochemistry, 56, 5967-5971 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.B7 gene cntM, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa
2.5.1.B47 gene cntL, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa
2.5.1.152 gene cntL, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.B7 additional information
-
additional information Michaelis-Menten steady-state kinetics Pseudomonas aeruginosa
2.5.1.B47 additional information
-
additional information Michaelis-Menten steady-state kinetics, stopped flow spectrometry Pseudomonas aeruginosa
2.5.1.B47 0.0054
-
L-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Pseudomonas aeruginosa
2.5.1.152 additional information
-
additional information Michaelis-Menten steady-state kinetics, stopped flow spectrometry Staphylococcus aureus
2.5.1.152 0.013
-
D-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa ATCC 15692 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa 1C i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa PRS 101 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa DSM 22644 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa CIP 104116 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa LMG 12228 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa JCM 14847 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa ATCC 15692
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa 1C
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa PRS 101
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa DSM 22644
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa CIP 104116
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa LMG 12228
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine Pseudomonas aeruginosa JCM 14847
-
N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
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
-
?
2.5.1.152 S-adenosyl-L-methionine + D-histidine Staphylococcus aureus Mu50
-
N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.B7 Pseudomonas aeruginosa Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa 1C Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa ATCC 15692 Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa CIP 104116 Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa DSM 22644 Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa JCM 14847 Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa LMG 12228 Q9HUX5
-
-
1.5.1.B7 Pseudomonas aeruginosa PRS 101 Q9HUX5
-
-
2.5.1.B47 Pseudomonas aeruginosa Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa 1C Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa ATCC 15692 Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa CIP 104116 Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa DSM 22644 Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa JCM 14847 Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa LMG 12228 Q9HUX4
-
-
2.5.1.B47 Pseudomonas aeruginosa PRS 101 Q9HUX4
-
-
2.5.1.152 Staphylococcus aureus A0A0H3JXA8
-
-
2.5.1.152 Staphylococcus aureus ATCC 700699 A0A0H3JXA8
-
-
2.5.1.152 Staphylococcus aureus Mu50 A0A0H3JXA8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.B7 recombinant His-tagged enzyme PaODH from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity Pseudomonas aeruginosa
2.5.1.B47 recombinant His-tagged enzyme PaNAS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity Pseudomonas aeruginosa
2.5.1.152 recombinant His-tagged enzyme SaNAS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity Staphylococcus aureus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.152 3.2
-
purified recombinant His-tagged enzyme, with pyruvate and D-histidine, NADPH oxidation, pH 8,0, 22°C Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa ATCC 15692 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa 1C pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa PRS 101 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa DSM 22644 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa CIP 104116 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa LMG 12228 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine Pseudomonas aeruginosa JCM 14847 pseudopaline + NADP+ + H2O
-
?
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa ATCC 15692 ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa 1C ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa PRS 101 ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa DSM 22644 ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa CIP 104116 ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa LMG 12228 ?
-
-
1.5.1.B7 additional information Pseudomonas aeruginosa ODH shows no catalytic activity in the presence of pyruvate or oxaloacetate (within error of zero), but full activity with 2-oxoglutarate. Coupled assay with enzyme nicotianamine synthase from Pseudomonas aeruginosa (PaNAS) and L-histidine. Substrate specificities, metabolite analysis by NMR, overview Pseudomonas aeruginosa JCM 14847 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa ATCC 15692 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa 1C ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa PRS 101 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa DSM 22644 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa CIP 104116 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa LMG 12228 ?
-
-
2.5.1.B47 additional information PaNAS is specific for L-histidine. Coupled assay with enzyme pseudopaline synthase from Pseudomonas aeruginosa (PaODH, EC 1.5.1.52). Substrate specificities, overview Pseudomonas aeruginosa JCM 14847 ?
-
-
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa ATCC 15692 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa 1C N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa PRS 101 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa DSM 22644 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa CIP 104116 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa LMG 12228 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.B47 S-adenosyl-L-methionine + L-histidine
-
Pseudomonas aeruginosa JCM 14847 N-[(3S)-3-amino-3-carboxypropyl]-L-histidine + S-methyl-5'-thioadenosine
-
?
2.5.1.152 additional information SaNAS is specific for D-histidine. Coupled assay with enzyme staphylopine synthase from Staphylococcus aureus (SaODH, EC 1.5.1.52). Substrate specificities, overview Staphylococcus aureus ?
-
-
2.5.1.152 additional information SaNAS is specific for D-histidine. Coupled assay with enzyme staphylopine synthase from Staphylococcus aureus (SaODH, EC 1.5.1.52). Substrate specificities, overview Staphylococcus aureus ATCC 700699 ?
-
-
2.5.1.152 additional information SaNAS is specific for D-histidine. Coupled assay with enzyme staphylopine synthase from Staphylococcus aureus (SaODH, EC 1.5.1.52). Substrate specificities, overview Staphylococcus aureus Mu50 ?
-
-
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
-
?
2.5.1.152 S-adenosyl-L-methionine + D-histidine
-
Staphylococcus aureus Mu50 N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.B7 cntM
-
Pseudomonas aeruginosa
1.5.1.B7 ODH
-
Pseudomonas aeruginosa
1.5.1.B7 PA4835
-
Pseudomonas aeruginosa
1.5.1.B7 PaODH
-
Pseudomonas aeruginosa
1.5.1.B7 pseudopaline synthase UniProt Pseudomonas aeruginosa
2.5.1.B47 cntL
-
Pseudomonas aeruginosa
2.5.1.B47 NAS
-
Pseudomonas aeruginosa
2.5.1.B47 PA4836
-
Pseudomonas aeruginosa
2.5.1.B47 PaNAS
-
Pseudomonas aeruginosa
2.5.1.152 cntL
-
Staphylococcus aureus
2.5.1.152 D-histidine 2-aminobutanoyltransferase UniProt Staphylococcus aureus
2.5.1.152 NAS
-
Staphylococcus aureus
2.5.1.152 nicotianamine synthase-like enzyme UniProt Staphylococcus aureus
2.5.1.152 SaNAS
-
Staphylococcus aureus
2.5.1.152 sav2468
-
Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.B7 22
-
assay at Pseudomonas aeruginosa
2.5.1.152 22
-
assay at Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.B47 0.0178
-
L-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Pseudomonas aeruginosa
2.5.1.152 0.298
-
D-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.B7 8
-
assay at Pseudomonas aeruginosa
2.5.1.B47 8
-
assay at Pseudomonas aeruginosa
2.5.1.152 8
-
assay at Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.B7 additional information lower affinity of PaODH for NADH, preferably PaODH binds NADPH Pseudomonas aeruginosa
1.5.1.B7 NADPH
-
Pseudomonas aeruginosa
2.5.1.B47 additional information lower affinity of PaODH for NADH, preferably PaODH binds NADPH Pseudomonas aeruginosa
2.5.1.B47 NADPH
-
Pseudomonas aeruginosa
2.5.1.152 NADPH
-
Staphylococcus aureus

General Information

EC Number General Information Comment Organism
1.5.1.B7 metabolism the NADPH is oxidized to NADP+ by the PaODH in the presence of Pseudomonas aeruginosa nicotianamine synthase (PaNAS), S-adenosyl-L-methionine (SAM) and the correct amino acid and 2-oxo acid substrates. Pyruvate, oxaloacetate, and 2-oxoglutarate are screened with SAM, but no oxidation is observed, suggesting that SAM alone is not sufficient as a substrate for PaNAS. Screening of 42 L- and D-amino acid substrates in combination with pyruvate, oxaloacetate, or 2-oxoglutarate reveals that several amino acids, L-threonine, L-asparagine, and L-hydroxyproline (L-Hyp), show limited turnover, while the combination of L-histidine and 2-oxoglutarate results in significant oxidation of NADPH by PaODH. PaNAS is specific for L-histidine Pseudomonas aeruginosa
1.5.1.B7 physiological function opine dehydrogenases (ODHs) typically form a secondary amine by condensation of an amino acid with an alpha-keto acid. Pseudomonas aeruginosa encodes the enzymes nicotianamine synthase (NAS) and opine dehydrogenase (ODH), biosynthesizing the nicotianamine-like opine metallophore pseudopaline Pseudomonas aeruginosa
2.5.1.B47 metabolism the NADPH is oxidized to NADP+ by the Pseudomonas aeruginosa opine dehydrogenase (PaODH, EC 1.5.1.52) in the presence of PaNAS, S-adenosyl-L-methionine (SAM) and the correct amino acid and 2-oxo acid substrates. The combination of L-histidine and 2-oxoglutarate results in significant oxidation of NADPH by PaODH Pseudomonas aeruginosa
2.5.1.B47 physiological function opine dehydrogenases (ODHs) typically form a secondary amine by condensation of an amino acid with an alpha-keto acid. Pseudomonas aeruginosa encodes the enzymes nicotianamine synthase (NAS) and opine dehydrogenase (ODH), biosynthesizing the nicotianamine-like opine metallophore pseudopaline. PaNAS is specific for L-histidine Pseudomonas aeruginosa
2.5.1.152 metabolism the NADPH is oxidized to NADP+ by the Staphylococcus aureus SaODH (EC 1.5.1.52) in the presence of nicotianamine synthase (PaNAS), S-adenosyl-L-methionine (SAM,) and the correct amino acid and 2-oxo acid substrates. The combination of D-histidine and pyruvate results in significant oxidation of NADPH by SaODH Staphylococcus aureus
2.5.1.152 physiological function opine dehydrogenases (ODHs) typically form a secondary amine by condensation of an amino acid with an alpha-keto acid. Staphylococcus aureus encodes the enzymes nicotianamine synthase (NAS) and opine dehydrogenase (ODH), biosynthesizing the nicotianamine-like opine metallophore staphylopaline. In Staphylococcus aureus, ODH uses the primary amine of the D-histidine-aminobutyrate product of NAS as a nucleophile in a condensation with pyruvate followed by hydride transfer from NADPH. SaNAS is specific for D-histidine Staphylococcus aureus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.B47 3.303
-
L-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Pseudomonas aeruginosa
2.5.1.152 22.92
-
D-histidine pH 8.0, 22°C, recombinant His-tagged enzyme Staphylococcus aureus