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Literature summary extracted from

  • 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 (2018), J. Biol. Chem., 293, 8009-8019 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.52 expression in Escherichia coli Staphylococcus aureus

Crystallization (Commentary)

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

KM Value [mM]

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

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 + 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
-
?

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
-
-
1.5.1.B8 Yersinia pestis Q8CKU7
-
-
1.5.1.52 Staphylococcus aureus A0A0H3JT80
-
-
1.5.1.52 Staphylococcus aureus ATCC 700699 A0A0H3JT80
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.52
-
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 + 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
-
?

Subunits

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

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
-
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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

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

General Information

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

kcat/KM [mM/s]

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