1.5.1.B7: pseudopaline synthase
This is an abbreviated version!
For detailed information about pseudopaline synthase, go to the full flat file.
Reaction
Synonyms
cntM, ODH, PA4835, PaODH, pseudopaline synthase
ECTree
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Substrates Products
Substrates Products on EC 1.5.1.B7 - pseudopaline synthase
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REACTION DIAGRAM
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
pseudopaline + NADP+ + H2O
-
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADH + H+
pseudopaline + NAD+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
-
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
?
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+
pseudopaline + NADP+ + H2O
i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine
-
-
r
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-
additional information
?
-
L-histidine nicotianamine is preferred over D-histidine nicotianamine, poor activity with D-histidine nicotianamine
-
-
-
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
-
-
-
additional information
?
-
full knowledge of opine metallophore stereochemistry is important as it is likely to influence receptor recognition as well as the coordination geometry for metal complexes. This is especially important for pseudopaline, because it incorporates an extra carboxylate ligand fromx022-oxoglutarate. As both PaODH and SaODH belong to the (R)-opine producing structural class, it is oproposed that they produce (R)-opine metallophores. The opine dehydrogenase reaction is reversible only for the opine metallophore product with (R)-stereochemistry at carbon C2 of the alpha-keto acid (prochiral prior to catalysis). Kinetic analysis using stopped-flow spectrometry with (R)- or (S)-staphylopine and kinetic and structural analysis with (R)- and (S)-pseudopaline confirms catalysis in the reverse direction for only (R)-staphylopine and (R)-pseudopaline, verifying the stereochemistry of these two opine metallophores. No NADP+ reduction with (S)-pseudopaline. Structural analysis at 1.57-1.85 A resolution captures the hydrolysis of (R)-pseudopaline and allows identification of a binding pocket for the L-histidine moiety of pseudopaline formed through a repositioning of Phe340 and Tyr289 during the catalytic cycle. Transient-state kinetic analysis reveals an ordered release of NADP+ followed by staphylopine, with staphylopine release being the rate-limiting step in catalysis. PaODH binds (S)-pseudopaline in a noncatalytic complex, (S)-pseudopaline binds above the nicotinamide ring of NADP+, structure analysis of enzyme-bound substrates, and reaction mechanism, detailed overview. PaODH crystals catalyze the hydrolysis of (R)-pseudopaline
-
-
-