Any feedback?
No. of entries
Information on EC 1.14.13.242 - 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
for references in articles please use BRENDA:EC1.14.13.242
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.242 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
IUBMB Comments
Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
The enzyme appears in viruses and cellular organisms
- 1.14.13.242
- flavin
- flavoproteins
- fad
- hydroxylases
-
mesorhizobium
-
flavoenzyme
-
electrophilic
- loti
-
acyclic
-
flavin-dependent
-
ring-cleavage
-
hydride
- isoalloxazine
Reaction Schemes
showSynonyms
mhpco, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, mlr6788, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase
-
-
-
-
2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
3-hydroxy-2-methylpyridine carboxylate dioxygenase
-
-
-
-
3-hydroxy-2-methylpyridinecarboxylate dioxygenase
-
-
misleading
-
EC 1.14.12.4
-
-
formerly
-
methylhydroxypyridine carboxylate dioxygenase
-
-
-
-
methylhydroxypyridinecarboxylate oxidase
-
-
-
-
MHPCO
mlr6788
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)+
reaction proceeds in a concerted fashion via a ternary complex of oxygenase, NADH and 3-hydroxy-2-methylpyridine-5-carboxylate
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
ordered mechanism in which 3-hydroxy-2-methylpyridine-5-carboxylate binds first, followed by NADH. The first product NAD+ is then released, followed by oxygen binding and finally release of the oxygenated and reduced cleavage product 2-(acetamidomethylene)succinate
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
the enzyme catalyzes both a classical hydroxylation and a subsequent unique hydrolysis of the hydroxylated substrate to yield the acyclic product
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
the binding proceeds in two steps: an enzyme-substrate complex initially formed is followed by a ligand-induced isomerization
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
oxygenation reaction occurs via an electrophilic aromatic substitution mechanism
-
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
vitamin B6 degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)
Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37256-69-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
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+
-
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinate + NAD(P)H + H+ + O2
? + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
Substrates: 5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
-
Substrates: the nitrogen atom of the 3-hydroxy-2-methylpyridine-5-carboxylate is invariably protonated during the catalytic reaction
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
Substrates: inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
Substrates: enzyme is involved in degradation of vitamin B6
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
Substrates: about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
Substrates: 5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
Products: -
Products: -
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
Substrates: 5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
Products: -
Products: -
?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
Substrates: 5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
Products: -
Products: -
?
additional information
?
-
Substrates: comparisons of substrate binding structure analysis mechanism
Products: -
Products: -
-
additional information
?
-
-
Substrates: comparisons of substrate binding structure analysis mechanism
Products: -
Products: -
-
additional information
?
-
Substrates: comparisons of substrate binding structure analysis mechanism
Products: -
Products: -
-
additional information
?
-
Substrates: comparisons of substrate binding structure analysis mechanism
Products: -
Products: -
-
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
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+
-
Substrates: -
Products: -
Products: -
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
Substrates: about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
Substrates: 5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylidene)succinate + NAD(P)+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
Substrates: inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
Products: -
Products: -
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
-
Substrates: enzyme is involved in degradation of vitamin B6
Products: -
Products: -
?
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
additional information
?
-
Substrates: also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
Km value 624 nM, one mol of the enzyme contains 1.93 mol of FAD
NADH
-
interacts with the holoenzyme in a slow catalytically irrelevant manner
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-methylnicotinic acid
-
competitive with 3-hydroxy-2-methylpyridine-5-carboxylate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
0.21
5-hydroxynicotinic acid
mutant enzyme Y270F, at pH 8.0 and 25°C
0.00056
N-methyl-5-hydroxynicotinic acid
-
calculation from stopped-flow data
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). A0A852TMD2_9ACTN
384
0
42029
TrEMBL
-