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Information on EC 1.1.1.97 - 3-hydroxybenzyl-alcohol dehydrogenase for references in articles please use BRENDA:EC1.1.1.97
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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
m-hydroxybenzyl alcohol (NADP) dehydrogenase, m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzylalcohol dehydrogenase,
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m-hydroxybenzyl alcohol (NADP) dehydrogenase
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m-hydroxybenzyl alcohol dehydrogenase
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m-hydroxybenzylalcohol dehydrogenase
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3-hydroxybenzyl alcohol + NADP+ = 3-hydroxybenzaldehyde + NADPH + H+
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3-hydroxybenzyl-alcohol:NADP+ oxidoreductase
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
3-methoxybenzyl alcohol + NADP+
3-methoxybenzaldehyde + NADPH
4-hydroxybenzyl alcohol + NADP+
4-hydroxybenzaldehyde + NADPH
benzyl alcohol + NADP+
benzaldehyde + NADPH
ethanol + NADP+
acetaldehyde + NADPH + H+
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29% activity compared to 3-hydroxybenzyl alcohol
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r
3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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reduction of 3-hydroxybenzaldehyde is clearly favoured
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-methoxybenzyl alcohol + NADP+
3-methoxybenzaldehyde + NADPH
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3-methoxybenzyl alcohol + NADP+
3-methoxybenzaldehyde + NADPH
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4-hydroxybenzyl alcohol + NADP+
4-hydroxybenzaldehyde + NADPH
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4-hydroxybenzyl alcohol + NADP+
4-hydroxybenzaldehyde + NADPH
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10% activity compared to 3-hydroxybenzyl alcohol
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benzyl alcohol + NADP+
benzaldehyde + NADPH
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benzyl alcohol + NADP+
benzaldehyde + NADPH
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20% activity compared to 3-hydroxybenzyl alcohol
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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3-hydroxybenzyl alcohol + NADP+
3-hydroxybenzaldehyde + NADPH
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diethyldicarbonate
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81% inhibition, NADP+ protects partly from inhibition
iodoacetic acid
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54% inhibition, NADPH and NADP+ protect from inhibition
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dithiothreitol
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1.0 mM and 10 mM, 56% increase in activity, enzyme activity in cell extracts
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0.05
3-Hydroxybenzyl alcohol
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0.57
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enzyme activity in crude extracts from cells grown on 3,5-xylenol
0.65
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enzyme activity in crude extracts from cells grown on 3-hydroxy-5-methylbenzoate
0.7
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enzyme activity in crude extracts from cells grown on gentisate
0.78
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enzyme activity in crude extracts from cells grown on m-hxdroxybenzoate
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brenda
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36000
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4 * 36000, SDS-PAGE
120000
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sedimentation equilibrium
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tetramer
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4 * 36000, SDS-PAGE
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14 min half-life of crude enzyme at 30°C in 100 mM Tris-HCl, pH 7.6, half-life is increased to 77 and 80 min by 2 mM MnCl2 and FeCl3 respectively, 3 mM NADPH increase half-life to 146 min
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ammonium sulfate, Bio-Gel A, 2',5'-ADP-agarose, DEAE-Sephacell, 2',5'-ADP-agarose
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streptomycin sulfate, ammonium sulfate, Sephadex G-200, 6.55fold purification
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Hopper, D.J.; Kemp, P.D.
Regulation of enzymes of the 3,5-xylenol-degradative pathway in Pseudomonas putida: evidence for a plasmid
J. Bacteriol.
142
21-26
1980
Pseudomonas putida
brenda
Scott, R.E.; Lam, K.S.; Gaucher, G.M.
Stabilization and purification of the secondary metabolism specific enzyme, m-hydroxybenzylalcohol dehydrogenase
Can. J. Microbiol.
32
167-175
1986
Penicillium urticae
brenda
Gaucher, G.M.
meta-Hydroxybenzyl-alcohol dehydrogenase
Methods Enzymol.
43
540-548
1975
Penicillium urticae
brenda
Forrester, P.I.; Gaucher, G.M.
m-hydroxybenzyl alcohol dehydrogenase from Penicillium uricae
Biochemistry
11
1108-1114
1972
Penicillium urticae
brenda
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