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Information on EC 1.5.1.B7 - pseudopaline synthase
for references in articles please use BRENDA:EC1.5.1.B7preliminary BRENDA-supplied EC number
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EC Tree
1.5.1.B7 pseudopaline synthaseSpecify your search results
The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa
Reaction Schemes
+
+
=
+
+
+
pseudopaline
+
+
=
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate
+
+
+
Synonyms
paodh, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cntM
ODH
PA4835
PaODH
pseudopaline synthase
cntM
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pseudopaline + NADP+ + H2O = (2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + 2-oxoglutarate + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
pseudopaline:NADP+ oxidoreductase [(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate]-forming
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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 + 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 + 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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
lower affinity of PaODH for NADH, preferably PaODH binds NADPH
-
additional information
-
lower affinity of PaODH for NADH, preferably PaODH binds NADPH
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
2-oxoglutarate
recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C
61
2-oxoglutarate
recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C
additional information
additional information
steady-state kinetic analysis, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics. The reverse reaction initiated with (R)-pseudopaline shows steady-state turnover with a kcat value about 60% slower than the previously published forward rates
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.71
NADH
recombinant enzyme, with 2-oxoglutarate and L-histidine nicotianamine, pH 8.0, 22°C
0.33
NADPH
recombinant enzyme, with 2-oxoglutarate and L-histidine nicotianamine, pH 8.0, 22°C
0.42
2-oxoglutarate
recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C
0.92
2-oxoglutarate
recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
2-oxoglutarate
recombinant enzyme, with NADH and L-histidine nicotianamine, pH 8.0, 22°C
0.03
2-oxoglutarate
recombinant enzyme, with NADPH and L-histidine nicotianamine, pH 8.0, 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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)
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
physiological function
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
-
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)
-
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
-
physiological function
-
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview
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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
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
-
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
-
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
-
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
-
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
-
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODH_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
433
0
47715
Swiss-Prot
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in apoform or in complex with substrates, products, and/or NADP+, hanging drop vapor diffusion method, mixing of 0.0015 ml of a 1.2 mg/ml protein solution with 0.0015 ml of well solution containing 100 mM Bis-Tris, pH 5.45, 200 mM ammonium acetate, and 24% PEG 3350, with NADP+, or 270-290 mM ammonium formate and 28% PEG 3350, with pseudopaline, 4°C, X-ray diffraction structure determination and analysis at 1.57-2.18 A resolution, molecular replacement and modelling
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme PaODH from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cntM, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
293
8009-8019
2018
Pseudomonas aeruginosa (Q9HUX5), Pseudomonas aeruginosa ATCC 15692 (Q9HUX5), Pseudomonas aeruginosa 1C (Q9HUX5), Pseudomonas aeruginosa PRS 101 (Q9HUX5), Pseudomonas aeruginosa DSM 22644 (Q9HUX5), Pseudomonas aeruginosa CIP 104116 (Q9HUX5), Pseudomonas aeruginosa LMG 12228 (Q9HUX5), Pseudomonas aeruginosa JCM 14847 (Q9HUX5)
brenda
McFarlane, J.S.; Lamb, A.L.
Biosynthesis of an opine metallophore by Pseudomonas aeruginosa
Biochemistry
56
5967-5971
2017
Pseudomonas aeruginosa (Q9HUX5), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HUX5), Pseudomonas aeruginosa 1C (Q9HUX5), Pseudomonas aeruginosa PRS 101 (Q9HUX5), Pseudomonas aeruginosa DSM 22644 (Q9HUX5), Pseudomonas aeruginosa CIP 104116 (Q9HUX5), Pseudomonas aeruginosa LMG 12228 (Q9HUX5), Pseudomonas aeruginosa JCM 14847 (Q9HUX5)
brenda
McFarlane, J.S.; Zhang, J.; Wang, S.; Lei, X.; Moran, G.R.; Lamb, A.L.
Staphylopine and pseudopaline dehydrogenase from bacterial pathogens catalyze reversible reactions and produce stereospecific metallophores
J. Biol. Chem.
294
17988-18001
2019
Pseudomonas aeruginosa (Q9HUX5), Pseudomonas aeruginosa ATCC 15692 (Q9HUX5), Pseudomonas aeruginosa 1C (Q9HUX5), Pseudomonas aeruginosa PRS 101 (Q9HUX5), Pseudomonas aeruginosa DSM 22644 (Q9HUX5), Pseudomonas aeruginosa CIP 104116 (Q9HUX5), Pseudomonas aeruginosa LMG 12228 (Q9HUX5), Pseudomonas aeruginosa JCM 14847 (Q9HUX5)
brenda
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Release 2023.1 (January 2023)
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