EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.52 | expression in Escherichia coli | Staphylococcus aureus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.5.1.B7 | purified recombinant wild-type PaODH complexed with NADP+, X-ray diffraction structure determination and analysis, single wavelength anomalous dispersion, at 1.95 A resolution, molecular replacement and modelling | Pseudomonas aeruginosa |
1.5.1.B8 | purified recombinant, wild-type or selenomethionine-labeled YpODH in apoform or complexed with NADP+, X-ray diffraction structure determination and analysis, single wavelength anomalous dispersion, at 2.15-2.85 A resolution, molecular replacement and modelling | Yersinia pestis |
1.5.1.52 | 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 | Staphylococcus aureus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.B7 | additional information | - |
additional information | steady-state kinetic analysis, overview | Pseudomonas aeruginosa | |
1.5.1.B7 | 14 | - |
2-oxoglutarate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B7 | 61 | - |
2-oxoglutarate | recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B8 | additional information | - |
additional information | steady-state kinetic analysis, overview | Yersinia pestis | |
1.5.1.B8 | 0.073 | - |
pyruvate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 1.9 | - |
oxaloacetate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 1.9 | - |
glyoxylate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.52 | 0.029 | - |
pyruvate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 1.4 | - |
oxaloacetate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 3 | - |
glyoxylate | pH 8.0, 22°C | Staphylococcus aureus |
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 + 2-oxoglutarate + NADPH + H+ | Pseudomonas aeruginosa | - |
pseudopaline + NADP+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | 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 + 2-oxoglutarate + NADPH + H+ | Pseudomonas aeruginosa JCM 14847 | - |
pseudopaline + NADP+ + H2O | - |
? | |
1.5.1.B8 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + pyruvate + NADPH + H+ | Yersinia pestis | - |
yersinopine + 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 | 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 | 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. 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 | staphylopine + NADP+ + H2O | - |
? |
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 | - |
- |
1.5.1.B8 | Yersinia pestis | Q8CKU7 | - |
- |
1.5.1.52 | Staphylococcus aureus | A0A0H3JT80 | - |
- |
1.5.1.52 | Staphylococcus aureus ATCC 700699 | A0A0H3JT80 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.1.52 | - |
Staphylococcus aureus |
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 + 2-oxoglutarate + NADPH + H+ | - |
Pseudomonas aeruginosa | pseudopaline + NADP+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
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 + 2-oxoglutarate + NADPH + H+ | - |
Pseudomonas aeruginosa JCM 14847 | pseudopaline + NADP+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa ATCC 15692 | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa 1C | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa PRS 101 | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa DSM 22644 | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa CIP 104116 | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa LMG 12228 | pseudopaline + NAD+ + H2O | - |
? | |
1.5.1.B7 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+ | i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine | Pseudomonas aeruginosa JCM 14847 | pseudopaline + NAD+ + 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 | 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 | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa 1C | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
1.5.1.B7 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
1.5.1.B8 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + glyoxylate + NADPH + H+ | - |
Yersinia pestis | ? + NADP+ + H2O | - |
? | |
1.5.1.B8 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ | - |
Yersinia pestis | ? + NADP+ + H2O | - |
? | |
1.5.1.B8 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + pyruvate + NADH + H+ | - |
Yersinia pestis | yersinopine + NAD+ + H2O | - |
? | |
1.5.1.B8 | (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + pyruvate + NADPH + H+ | - |
Yersinia pestis | yersinopine + NADP+ + H2O | - |
? | |
1.5.1.B8 | additional information | L-histidine nicotianamine is preferred over D-histidine nicotianamine, no activity with D-histidine nicotianamine | Yersinia pestis | ? | - |
- |
|
1.5.1.52 | (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+ | the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | Staphylococcus aureus | ? + NADP+ + H2O | - |
? | |
1.5.1.52 | (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + glyoxylate + NADPH + H+ | the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | Staphylococcus aureus ATCC 700699 | ? + NADP+ + H2O | - |
? | |
1.5.1.52 | (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+ | the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | Staphylococcus aureus | ? + NADP+ + H2O | - |
? | |
1.5.1.52 | (2S)-2-amino-4-[[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino]butanoate + oxaloacetate + NADPH + H+ | the enzyme prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | Staphylococcus aureus ATCC 700699 | ? + 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. 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 | 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 prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | 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. 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 | 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 prefers the alpha-oxo acid substrate pyruvate but also exhibits limited turnover with oxaloacetate and glyoxylate | Staphylococcus aureus ATCC 700699 | staphylopine + NADP+ + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.B8 | dimer | YpODH is composed of three domains. NADPH binds along a canonical GXGXXA loop within the N-terminal NAD(P)H-binding domain. This domain forms one half of the active site. The other half, and the proposed location for substrate binding, is formed by the catalytic domain. These domains are separated by a central cleft. Embedded within the catalytic domain is a third domain that forms a dimerization interface. The NAD(P)H-binding domain has a Rossmann-like fold. This domain contains twelve beta-strands, five alpha-helices, and one 310 helix. Helix G acts as a linker connecting the NAD(P)H-binding domain with the C-terminal, predominantly alpha-helical, domains, structure overview | Yersinia pestis |
1.5.1.52 | dimer | - |
Staphylococcus aureus |
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 | - |
Pseudomonas aeruginosa |
1.5.1.B8 | ODH | - |
Yersinia pestis |
1.5.1.B8 | opine dehydrogenase | - |
Yersinia pestis |
1.5.1.B8 | YpODH | - |
Yersinia pestis |
1.5.1.52 | SaODH | - |
Staphylococcus aureus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.1.B7 | 22 | - |
assay at | Pseudomonas aeruginosa |
1.5.1.B8 | 22 | - |
assay at | Yersinia pestis |
1.5.1.52 | 22 | - |
assay at | Staphylococcus aureus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.B7 | 0.33 | - |
NADPH | recombinant enzyme, with 2-oxoglutarate and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B7 | 0.42 | - |
2-oxoglutarate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B7 | 0.71 | - |
NADH | recombinant enzyme, with 2-oxoglutarate and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B7 | 0.92 | - |
2-oxoglutarate | recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B8 | 0.013 | - |
NADH | recombinant enzyme, with pyruvate and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 0.22 | - |
glyoxylate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 0.29 | - |
oxaloacetate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 0.3 | - |
pyruvate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 0.38 | - |
NADPH | recombinant enzyme, with pyruvate and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.52 | 0.074 | - |
glyoxylate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 0.26 | - |
NADPH | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 0.26 | - |
pyruvate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 0.26 | - |
oxaloacetate | pH 8.0, 22°C | Staphylococcus aureus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.1.B7 | 8 | - |
assay at | Pseudomonas aeruginosa |
1.5.1.B8 | 8 | - |
assay at | Yersinia pestis |
1.5.1.52 | 8 | - |
assay at | Staphylococcus aureus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.B7 | additional information | significant catalysis is also observed for PaODH with NADH, the kcat of PaODH is 2.2fold higher than the kcat for NADPH. PaODH is nonspecific for the NAD(P)H substrate | Pseudomonas aeruginosa | |
1.5.1.B7 | NADH | - |
Pseudomonas aeruginosa | |
1.5.1.B7 | NADP+ | binding structure, overview | Pseudomonas aeruginosa | |
1.5.1.B7 | NADPH | - |
Pseudomonas aeruginosa | |
1.5.1.B8 | additional information | YpODH shows little turnover with NADH and a 26fold lower kcat compared to NADPH | Yersinia pestis | |
1.5.1.B8 | NADP+ | binding structure, overview | Yersinia pestis | |
1.5.1.B8 | NADPH | - |
Yersinia pestis | |
1.5.1.52 | NADPH | the enzyme is specific for NADPH | Staphylococcus aureus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.B7 | metabolism | opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Comparison of structure-function relationships, overview | Pseudomonas aeruginosa |
1.5.1.B7 | additional information | structure-function analysis, stereochemic reaction, overview. Active site structure involving Asp153 and substrate binding analysis. The histidine is positioned to act as a general acid/general base deprotonating the nucleophile and then donating the proton back to the 2-carbon hydroxyl leading to water release and Schiff base formation. HisNA is oriented with the imidazole moiety deep in the active site to confer stereoselectivity. This places the primary amine of the aminobutyrate proximal to the plane between the hydride and His242, positioning the substrate for nucleophilic attack. The nicotinamide ring hydride is 8.5 A distant from the histidine proton, too far for catalysis, further supporting the necessity of domain closure | Pseudomonas aeruginosa |
1.5.1.B7 | physiological function | opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Important role for this pathway in metal acquisition and virulence in humans, including in lung and burn-wound infections (Pseudomonas aeruginosa) and in blood and heart infections (Staphylococcus aureus) | Pseudomonas aeruginosa |
1.5.1.B8 | metabolism | opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Comparison of structure-function relationships, overview | Yersinia pestis |
1.5.1.B8 | additional information | structure-function analysis, stereochemic reaction, overview. Active site structure involving Asp153 and substrate binding analysis. The histidine is positioned to act as a general acid/general base deprotonating the nucleophile and then donating the proton back to the 2-carbon hydroxyl leading to water release and Schiff base formation. HisNA is oriented with the imidazole moiety deep in the active site to confer stereoselectivity. This places the primary amine of the amino butyrate proximal to the plane between the hydride and His242, positioning the substrate for nucleophilic attack. The nicotinamide ring hydride is 8.5 A distant from the histidine proton, too far for catalysis, further supporting the necessity of domain closure | Yersinia pestis |
1.5.1.B8 | physiological function | opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Important role for this pathway in metal acquisition and virulence | Yersinia pestis |
1.5.1.52 | 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 | Staphylococcus aureus |
1.5.1.52 | 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 | Staphylococcus aureus |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.B7 | 0.015 | - |
2-oxoglutarate | recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B7 | 0.03 | - |
2-oxoglutarate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Pseudomonas aeruginosa | |
1.5.1.B8 | 0.12 | - |
glyoxylate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 0.15 | - |
oxaloacetate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.B8 | 4.11 | - |
pyruvate | recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C | Yersinia pestis | |
1.5.1.52 | 0.024 | - |
glyoxylate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 0.18 | - |
oxaloacetate | pH 8.0, 22°C | Staphylococcus aureus | |
1.5.1.52 | 8.9 | - |
pyruvate | pH 8.0, 22°C | Staphylococcus aureus |