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IUBMB Comments Also oxidizes 2,5-dihydroxypyridine, but does not act on 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine.
Synonyms
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2-hydroxypyridine oxygenase
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HpdABCDE
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
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SDIMO
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
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2-hydroxypyridine + reduced acceptor + O2 = 2,5-dihydroxypyridine + acceptor + H2O
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2-hydroxypyridine,hydrogen-donor:oxygen oxidoreductase (5-hydroxylating)
Also oxidizes 2,5-dihydroxypyridine, but does not act on 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine.
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2-hydroxypyridine + NADH + O2
2,5-dihydroxypyridine + NAD+ + H2O
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Substrates: -
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2-hydroxypyridine + reduced acceptor + O2
2,5-dihydroxypyridine + acceptor + H2O
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
Substrates: -
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2-hydroxypyridine + NADH + O2
2,5-dihydroxypyridine + NAD+ + H2O
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Substrates: -
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Ferredoxin
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
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NADPH
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2% activity of NADH
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FMN
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85% inhibition at 1.7 mM, 2 min preincubation
Na2As2O3
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partial inhibition
NaF
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53% inhibition at 1.7 mM, 5 min preincubation
NaN3
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53% inhibition at 1.7 mM, 5 min preincubation
NiCl2
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47% inhibition at 1.7 mM
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6.3 - 8.5
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half-maximal activity at pH 6.3 and pH 8.5
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isolated by enrichment on isonicotinic acid
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brenda
A0A2R4K2I2 i.e. monooxygenase subunit HpdA, A0A2R4K2J6 i.e. monooxygenase regulatory subunit HpdB, A0A2R4K2J8 i.e. monooxygenase catalytic subunit HpdC, A0A2R4K2J7 i.e. ferredoxin subunit HpdD, A0A2R4K2J9 i.e. NADH-ubiquinone oxidoreductase subunit HpdE
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
UniProt
brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
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physiological function
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
HpdABCDE catalyzes the enzymatic turnover of 2-hydroxypyridine to 2,5-dihydroxypyridine. Emerging 2,5-dihydroxypyridine is a substrate for HpdF, an enzyme similar to 2,5-dihydroxypyridine 5,6-dioxygenases involved in the catabolic pathways of nicotine and nicotinic acid
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45 mM dithiothreitol affords partial protection against denaturation
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50% glycerol affords partial protection against denaturation
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dialysis of extracts in cold, 4°C, against phosphate buffer, pH 7.0, 0.05 M, for 4 h, 90% activity loss
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enzyme is completely blocked by anaerobic conditions
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-10°C or 0°C, overnight, complete loss of activity
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-20°C, Tris HCl buffer, pH 7.4, 0.05 M, 10% ethanol, 50% glycerol, 0.045 M dithiothreitol, 1 mM 2-mercaptoethanol, stable for 16 d
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expression in Burkholderia sp. MAK1 and in Escherichia coli
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
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the transcription of HpdABCDE genes increases 100fold in the presence of 2-hydroxypyridine
A0A2R4K2I2; A0A2R4K2J6; A0A2R4K2J8; A0A2R4K2J7; A0A2R4K2J9
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degradation
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in industrial wastewaters, pyridine biodegradation is initiated by two monooxygenation reactions that compete for intracellular electron donor (2H). UV photolysis of pyridine generates succinate, whose oxidation augments the intracellular electron donor and accelerates pyridine biodegradation and mineralization. The first monooxygenation reaction of pyridine to 2-hydroxypyridine always is faster than the second one, because electrons provided by intracellular electron donors are preferentially utilized by the first monooxygenase
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Sharma, M.L.; Kaul, S.M.; Shukla, O.P
Metabolism of 2-hydroxypyridine by Bacillus brevis (INA)
Biol. Mem.
9
43-52
1984
Brevibacillus brevis
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brenda
Petkevicius, V.; Vaitekunas, J.; Stankeviciute, J.; Gasparaviciute, R.; Meskys, R.
Catabolism of 2-hydroxypyridine by Burkholderia sp. strain MAK1 A 2-hydroxypyridine 5-monooxygenase encoded by hpdABCDE catalyzes the first step of biodegradation
Appl. Environ. Microbiol.
84
e00387-18
2018
Burkholderia sp. MAK1 (A0A2R4K2I2 and A0A2R4K2J6 and A0A2R4K2J8 and A0A2R4K2J7 and A0A2R4K2J9)
brenda
Yang, C.; Tang, Y.; Xu, H.; Yan, N.; Li, N.; Zhang, Y.; Rittmann, B.E.
Competition for electrons between mono-oxygenations of pyridine and 2-hydroxypyridine
Biodegradation
29
419-427
2018
uncultured bacterium
brenda
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