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Literature summary for 1.5.1.B7 extracted from

  • 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 (2019), J. Biol. Chem., 294, 17988-18001 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.B7

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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 Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa ATCC 15692 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa 1C i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa PRS 101 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa DSM 22644 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa CIP 104116 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa LMG 12228 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r
(2S)-2-amino-4-([(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino)butanoate + oxaloacetate + NADPH + H+ Pseudomonas aeruginosa JCM 14847 i.e. N-[(3S)-3-amino-3-carboxypropyl]-L-histidine pseudopaline + NADP+ + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HUX5
-
-
Pseudomonas aeruginosa 1C Q9HUX5
-
-
Pseudomonas aeruginosa ATCC 15692 Q9HUX5
-
-
Pseudomonas aeruginosa CIP 104116 Q9HUX5
-
-
Pseudomonas aeruginosa DSM 22644 Q9HUX5
-
-
Pseudomonas aeruginosa JCM 14847 Q9HUX5
-
-
Pseudomonas aeruginosa LMG 12228 Q9HUX5
-
-
Pseudomonas aeruginosa PRS 101 Q9HUX5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
-
 r
(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
-
 r
(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
-
 r
(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
-
 r
(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
-
 r
(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
-
 r
(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
-
 r
(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
-
 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 Pseudomonas aeruginosa ?
-
-
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 Pseudomonas aeruginosa ATCC 15692 ?
-
-
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 Pseudomonas aeruginosa 1C ?
-
-
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 Pseudomonas aeruginosa PRS 101 ?
-
-
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 Pseudomonas aeruginosa DSM 22644 ?
-
-
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 Pseudomonas aeruginosa CIP 104116 ?
-
-
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 Pseudomonas aeruginosa LMG 12228 ?
-
-
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 Pseudomonas aeruginosa JCM 14847 ?
-
-

Synonyms

Synonyms Comment Organism
cntM
-
 Pseudomonas aeruginosa
ODH
-
 Pseudomonas aeruginosa
PA4835
-
 Pseudomonas aeruginosa
PaODH
-
 Pseudomonas aeruginosa
pseudopaline synthase UniProt Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
24
-
 assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Pseudomonas aeruginosa
NADPH
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview Pseudomonas aeruginosa