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IUBMB Comments The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.
Synonyms
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glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase
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L-(+)-glycol:NAD(P) oxidoreductase
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L-glycol dehydrogenase (NAD+)
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L-glycol:NAD(P) dehydrogenase
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an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
glyoxal reduction by enzyme form pI 7.2 follows ordered bi-bi mechanism in which the coenzyme is the first substrate to bind to the enzyme
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an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
ordered bi-bi-mechanism, coenzyme binds as first substrate to the enzyme
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an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
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L-glycol:NAD(P)+ oxidoreductase
The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.
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2,3-pentanedione + NADH
L-acetylethylcarbinol + NAD+
diacetyl + NADH
L-acetoin + NAD+
ethyl pyruvate + NAD(P)H
ethyl lactate
glyceraldehyde + NADPH + H+
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Substrates: -
r
glyoxal + NADPH + H+
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Substrates: -
r
methyl pyruvate + NAD(P)H
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Substrates: -
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methylglyoxal + NADH
L-lactaldehyde
R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
R1-CO-CO-R2 + NAD(P)H
R1-CO-CHOH-R2 + NAD(P)+
additional information
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Substrates: not: acetaldehyde, monoketones, non-vicinal diketones, free ketoacids
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2,3-pentanedione + NADH
L-acetylethylcarbinol + NAD+
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Substrates: -
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2,3-pentanedione + NADH
L-acetylethylcarbinol + NAD+
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Substrates: -
ir
diacetyl + NADH
L-acetoin + NAD+
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Substrates: -
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diacetyl + NADH
L-acetoin + NAD+
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Substrates: -
ir
ethyl pyruvate + NAD(P)H
ethyl lactate
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Substrates: -
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ethyl pyruvate + NAD(P)H
ethyl lactate
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Substrates: -
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methylglyoxal + NADH
L-lactaldehyde
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Substrates: -
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methylglyoxal + NADH
L-lactaldehyde
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Substrates: -
ir
R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
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Substrates: -
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R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
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Substrates: 2-hydroxycarbonyl compound e.g. glycolaldehyde, glyceraldehyde, acetoin, acetylethylcarbinol, diacetylmethylcarbinol
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R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
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Substrates: much more efficient in dehydrogenase direction
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R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
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Substrates: 2-hydroxycarbonyl compound e.g. glycolaldehyde, glyceraldehyde, acetoin, acetylethylcarbinol, diacetylmethylcarbinol
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R1-CO-CHOH-R2 + NAD(P)H
R1-CHOH-CHOH-R2 + NAD(P)+
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Substrates: much more efficient in dehydrogenase direction
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R1-CO-CO-R2 + NAD(P)H
R1-CO-CHOH-R2 + NAD(P)+
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Substrates: methylglyoxal, diacetyl, 2,3-pentanedione
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R1-CO-CO-R2 + NAD(P)H
R1-CO-CHOH-R2 + NAD(P)+
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Substrates: vicinal dicarbonyl: e.g. glyoxal
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R1-CO-CO-R2 + NAD(P)H
R1-CO-CHOH-R2 + NAD(P)+
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Substrates: methylglyoxal, diacetyl, 2,3-pentanedione
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additional information
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no activity with alpha-NADH
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NAD+
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NADH
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L-acetoin
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probably all L(+)-alpha-hydroxycarbonyls products inhibit uncompetitively at non-saturated concentrations
NAD+
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competitive inhibition for NADH
acetone
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pI 7.2 form
acetone
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uncompetitive for NADH
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0.035 - 10
2,3-Pentanedione
0.026 - 0.566
glyceraldehyde
additional information
additional information
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0.035
2,3-Pentanedione
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0.06
2,3-Pentanedione
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pI 7.2 form
0.097
2,3-Pentanedione
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pI 6.2 form
0.675
2,3-Pentanedione
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pI 4.8 form
2.013
acetoin
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pI 6.2 form
2.164
acetoin
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pI 4.8 form
2.59
acetoin
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pI 7.2 form
0.109
diacetyl
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pI 7.2 form
0.12
diacetyl
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pI 7.2 form
0.38
diacetyl
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pI 6.2 form
0.026
glyceraldehyde
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pI 7.2 form
0.026
glyceraldehyde
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enzyme form of pI 7.2, at pH 7.0 and 25°C
0.029
glyceraldehyde
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pI 6.2 form
0.029
glyceraldehyde
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enzyme form of pI 6.2, at pH 7.0 and 25°C
0.566
glyceraldehyde
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pI 4.8 form
0.566
glyceraldehyde
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enzyme form of pI 4.8, at pH 7.0 and 25°C
0.053
Glyoxal
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pI 6.2 form
0.053
Glyoxal
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enzyme form of pI 6.2, at pH 7.0 and 25°C
0.41
Glyoxal
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pI 7.2 form
0.411
Glyoxal
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pI 4.8 form
0.411
Glyoxal
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enzyme form of pI 4.8, at pH 7.0 and 25°C
0.522
Glyoxal
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pI 7.2 form
0.522
Glyoxal
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enzyme form of pI 7.2, at pH 7.0 and 25°C
0.09
methylglyoxal
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pI 7.2 form
0.098
methylglyoxal
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pI 6.2 form
0.102
methylglyoxal
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pI 7.2 form
0.006
NADH
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with ethyl pyruvate
0.0062
NADH
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with 2,3-pentadione
0.0088
NADH
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with diacetyl
0.0097
NADH
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with methylglyoxal
0.0022
NADPH
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with 2,3-pentanedione
0.0024
NADPH
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with glyoxal
0.0028
NADPH
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with methylglyoxal
0.0031
NADPH
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with diacetyl
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additional information
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25
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assay at
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hen
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brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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7
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very stable in both water and low molarity buffers of pH 7 at 0-4°C
286134, 286135
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easily inactivated in high molarity buffers
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very stable in both water and low molarity buffers of pH 7 at 0-4°C
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-18°C, enzyme at any stage of purification
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3 enzyme forms: pI 7.2, pI 6.2 and pI 4.8
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Bernardo, A.; Burgos, J.; Martin, R.
Purification and some properties of L-glycol dehydrogenase from hens muscle
Biochim. Biophys. Acta
659
189-198
1981
Gallus gallus
brenda
Burgos, J.; Sarmiento, R.M.
L-Glycol dehydrogenase from hen muscle
Methods Enzymol.
89
523-526
1982
Gallus gallus
brenda
Prieto, J.G.; Sarmiento, R.M.; Burgos, J.
Kinetics of alpha-dicarbonyls reduction by L-glycol dehydrogenase from hen muscle
Arch. Biochem. Biophys.
224
372-377
1983
Gallus gallus
brenda
Carballo, J.; Bernardo, A.; Prieto, M.J.G.; Sarmiento, R.M.
Kinetics of alpha-dicarbonyls reduction by L-glycol dehydrogenase (NAD+) from Enterobacter aerogenes
Ital. J. Biochem.
42
79-89
1993
Klebsiella aerogenes
brenda
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