Information on EC 1.14.12.4 - 3-hydroxy-2-methylpyridinecarboxylate dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.12.4
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxy-2-methylpyridinecarboxylate dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylene)succinate + NAD(P)+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vitamin B6 degradation
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-
Vitamin B6 metabolism
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-
Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-69-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylene)succinate + NAD(P)+
show the reaction diagram
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
show the reaction diagram
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
show the reaction diagram
5-hydroxynicotinate + NAD(P)H + H+ + O2
? + NAD(P)+
show the reaction diagram
5-hydroxynicotinic acid + NADH + O2
?
show the reaction diagram
5-pyridoxic acid + NADH + O2
?
show the reaction diagram
-
-
-
-
?
N-methyl-5-hydroxynicotinic acid + NADH + O2
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ion required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deaza-FAD
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-
5-pyridoxic acid
6-Methylnicotinate
-
-
6-methylnicotinic acid
-
competitive with 3-hydroxy-2-methylpyridine-5-carboxylate
NAD+
-
binds competitively with O2, but not with NADH
p-chloromercuribenzoate
-
; 0.05 mM, quick and complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.068
5-hydroxynicotinic acid
0.00056 - 0.0011
N-methyl-5-hydroxynicotinic acid
0.0054 - 0.205
NADH
0.0059 - 0.148
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00046
1-deaza-FAD
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-
0.023
5-pyridoxic acid
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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-
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
equilibrium sedimentation
166000
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equilibrium sedimentation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
crystal structure, the tetramer may have been disrupted
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
density functional theory/molecular mechanics calculations show that the active-site residues Arg211 and Tyr223 have a minor effect on the reaction, while the peptide bond of Pro295-Ala296, the side chain of Tyr82 and several crystal water molecules affect the reaction energy profile considerably. The ring-opening pathway, in which an epoxy transition state is formed, is more favored than the direct C2-C3 cleavage pathway. Both the reaction barriers for the hydroxylation and the ring-opening pathways are sensitive to the quantum mechanics/molecular mechanics partitioning
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is very sensitive to oxidation, it loses activity rapidly in absence of mercaptoethanol even at 4°C, it is further stabilized in presence of high concentrations of glycerol or by serum albumin
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439056
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, 0.1% 2-mercaptoethanol, 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
His-tag, expressed in Escherichia coli