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2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADPH + H+ + O2
2-(acetamidomethylene)succinate + NADP+
-
-
-
-
?
5-hydroxynicotinate + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
-
-
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
5-hydroxynicotinic acid + NADH + O2
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5-pyridoxic acid + NADH + O2
?
-
-
-
-
?
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
N-methyl-5-hydroxynicotinic acid + NADH + O2
?
-
-
-
-
?
additional information
?
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
the nitrogen atom of the 3-hydroxy-2-methylpyridine-5-carboxylate is invariably protonated during the catalytic reaction
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
enzyme is involved in degradation of vitamin B6
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
-
-
-
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
-
-
-
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
-
-
-
?
5-hydroxynicotinic acid + NADH + O2
?
-
-
-
-
?
5-hydroxynicotinic acid + NADH + O2
?
-
-
-
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
-
-
-
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
-
-
-
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
-
-
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
-
-
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
-
-
?
additional information
?
-
comparisons of substrate binding structure analysis mechanism
-
-
-
additional information
?
-
-
comparisons of substrate binding structure analysis mechanism
-
-
-
additional information
?
-
comparisons of substrate binding structure analysis mechanism
-
-
-
additional information
?
-
comparisons of substrate binding structure analysis mechanism
-
-
-
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
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2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADPH + H+ + O2
2-(acetamidomethylene)succinate + NADP+
-
-
-
-
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
-
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
-
-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
enzyme is involved in degradation of vitamin B6
-
-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
-
?
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physiological function
conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid to alpha-(N-acetylaminomethylene)succinic acid is the essential ring-opening step in the bacterial degradation of vitamin B6. The rearomatisation of the hydroxylated intermediate occurs spontaneously in aqueous solution. This implies that the ring-opening process occurs inside the enzyme's active site. Proposal of two pathways with reasonable energy barriers
physiological function
MHPCO is essential for the assimilation of pyridoxine, but not for its growth in a nutrient-rich medium. MHPCO is dispensable for at least nodule formation on roots of seedlings in symbiosis
physiological function
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) is a flavoenzyme that catalyzes oxidative ring opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid
physiological function
-
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) is a flavoenzyme that catalyzes oxidative ring opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
physiological function
-
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) is a flavoenzyme that catalyzes oxidative ring opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid
-
physiological function
-
conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid to alpha-(N-acetylaminomethylene)succinic acid is the essential ring-opening step in the bacterial degradation of vitamin B6. The rearomatisation of the hydroxylated intermediate occurs spontaneously in aqueous solution. This implies that the ring-opening process occurs inside the enzyme's active site. Proposal of two pathways with reasonable energy barriers
-
physiological function
-
MHPCO is essential for the assimilation of pyridoxine, but not for its growth in a nutrient-rich medium. MHPCO is dispensable for at least nodule formation on roots of seedlings in symbiosis
-
additional information
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO, PDB ID 5hxi) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
additional information
-
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO, PDB ID 5hxi) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
additional information
-
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO, PDB ID 5hxi) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
-
additional information
-
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO, PDB ID 5hxi) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
-
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Y223E
-
the mutant shows reduced activity compared to the wild type enzyme
Y223F
-
the mutant shows reduced activity compared to the wild type enzyme
Y223H
-
the mutant shows reduced activity compared to the wild type enzyme
Y223T
-
the mutant shows reduced activity compared to the wild type enzyme
Y82F
-
the mutant shows reduced activity compared to the wild type enzyme
Y82H
-
the mutant shows reduced activity compared to the wild type enzyme
Y82R
-
the mutant shows reduced activity compared to the wild type enzyme
Y270A
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270A
less than 0.1% of the pyridine ring cleavage capacity of wild-type
Y270F
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270F
about 1.5% of the pyridine ring cleavage capacity of wild-type
Y270A
-
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
-
Y270A
-
less than 0.1% of the pyridine ring cleavage capacity of wild-type
-
Y270F
-
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
-
Y270F
-
about 1.5% of the pyridine ring cleavage capacity of wild-type
-
Y270A
-
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
-
Y270A
-
less than 0.1% of the pyridine ring cleavage capacity of wild-type
-
Y270F
-
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
-
Y270F
-
about 1.5% of the pyridine ring cleavage capacity of wild-type
-
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Sparrow, L.G.; Ho, P.P.K.; Sundaram, T.K.; Zach, D.; Nyns, E.J.; Snell, E.E.
The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring
J. Biol. Chem.
244
2590-2600
1969
Pseudomonas sp.
brenda
Kishore, G.M.; Snell, E.E.
Interaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase with FAD, substrates, and analogues. Spectral and fluorescence investigations
J. Biol. Chem.
256
4234-4240
1981
Pseudomonas sp.
brenda
Kishore, G.M.; Snell, E.E.
Kinetic investigations on a flavoprotein oxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
J. Biol. Chem.
256
4228-4233
1981
Pseudomonas sp.
brenda
Chaiyen, P.; Ballou, D.P.; Massey, V.
Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Proc. Natl. Acad. Sci. USA
94
7233-7238
1997
Pseudomonas sp. (O08453), Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase with N-methyl-5-hydroxynicotinic acid: studies on the mode of binding, and Protonation Status of the Substrate
Biochemistry
36
13856-13864
1997
Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Unusual mechanism of oxygen atom transfer and product rearrangement in the catalytic reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
36
8060-8070
1997
Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Thermodynamics and reduction kinetics properties of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
36
2612-2621
1997
Pseudomonas sp.
brenda
Oonanant, W.; Sucharitakul, J.; Yuvaniyama, J.; Chaiyen, P.
Crystallization and preliminary x-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1
Acta Crystallogr. Sect. F
61
312-314
2005
Pseudomonas sp.
brenda
Chaiyen, P.; Sucharitakul, J.; Svasti, J.; Entsch, B.; Massey, V.; Ballou, D.P.
Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
43
3933-3943
2004
Pseudomonas sp.
brenda
McCulloch, K.; Mukherjee, T.; Begley, T.; Ealick, S.
Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications
Biochemistry
48
4139-4149
2009
Mesorhizobium loti (Q988D3)
brenda
Tian, B.; Strid, A.; Eriksson, L.A.
Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study
J. Phys. Chem. B
115
1918-1926
2011
Mesorhizobium loti, Mesorhizobium loti MAFF303099
brenda
Luanloet, T.; Sucharitakul, J.; Chaiyen, P.
Selectivity of substrate binding and ionization of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
FEBS J.
282
3107-3125
2015
Pseudomonas sp. MA-1
brenda
Kobayashi, J.; Yoshida, H.; Yagi, T.; Kamitori, S.; Hayashi, H.; Mizutani, K.; Takahashi, N.; Mikami, B.
Role of the Tyr270 residue in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti
J. Biosci. Bioeng.
123
154-162
2017
Mesorhizobium loti (Q988D3), Mesorhizobium loti, Mesorhizobium loti MAFF 303099 (Q988D3), Mesorhizobium loti MAFF303099 (Q988D3)
brenda
Tian, B.; Tu, Y.; Strid, A.; Eriksson, L.A.
Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase a theoretical study
Chemistry
16
2557-2566
2010
Mesorhizobium loti (Q988D3), Mesorhizobium loti MAFF 303099 (Q988D3)
brenda
Yuan, B.; Yokochi, N.; Yoshikane, Y.; Ohnishi, K.; Yagi, T.
Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti
J. Biosci. Bioeng.
102
504-510
2006
Mesorhizobium loti (Q988D3), Mesorhizobium loti, Mesorhizobium loti MAFF 303099 (Q988D3)
brenda
Lazar, J.T.; Shuvalova, L.; Rosas-Lemus, M.; Kiryukhina, O.; Satchell, K.J.F.; Minasov, G.
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases
Acta Crystallogr. F Struct. Biol. Commun.
75
507-514
2019
Mesorhizobium japonicum (Q988D3), Mesorhizobium japonicum, Mesorhizobium japonicum CECT 9101 (Q988D3)
brenda
Lazar, J.T.; Shuvalova, L.; Rosas-Lemus, M.; Kiryukhina, O.; Satchell, K.J.F.; Minasov, G.
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases
Acta Crystallogr. Sect. F
75
507-514
2019
Mesorhizobium japonicum (Q988D3), Mesorhizobium japonicum, Mesorhizobium japonicum LMG 29417 (Q988D3), Mesorhizobium japonicum CECT 9101 (Q988D3)
brenda