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EC Tree
IUBMB Comments The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
(indol-3-yl)lactate:NAD+ oxidoreductase, (R)-aromatic lactate dehydrogenase, D-aryllactate D-hydrogenase, indolelactate dehydrogenase,
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(indol-3-yl)lactate:NAD+ oxidoreductase
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(R)-aromatic lactate dehydrogenase
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D-aryllactate D-hydrogenase
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indolelactate dehydrogenase
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(R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+
(3)
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(R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
(R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
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(R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
(2)
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aromatic 2-oxoacid:NAD+ oxidoreductase
The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
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2-ketoisopentanoate + NAD(P)H
2-hydroxyisopentanoate + NAD(P)+
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poor substrate
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r
2-oxobutyrate + NAD(P)H + H+
2-hydroxybutyrate + NAD(P)+
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poor substrate
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r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
indoleglycolate + NAD+
indoleglyoxylate + NADH
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r
indolelactate + NAD+
indolepyruvate + NADH
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r
indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
p-hydroxyphenyllactate + NAD+
p-hydroxyphenylpyruvate + NADH
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r
phenyllactate + NAD+
phenylpyruvate + NADH
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r
phenylpyruvate + NAD(P)H
D-phenyllactate + NAD(P)+
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reduction at 27% the rate of p-hydroxyphenylpyruvate reduction
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r
pyruvate + NAD(P)H + H+
lactate + NAD(P)+
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poor substrate
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r
additional information
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best substrate for oxidation is p-hydroxyphenyllactate, D-phenyllactate is oxidized at 75% and indolelactate at 52% the rate of p-hydroxyphenyllactate
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?
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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the initial rate of oxidation is 100 fold lower than that of reduction
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r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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involved in aromatic amino acid catabolism
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?
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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involved in aromatic amino acid catabolism
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?
indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
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reduction at 30% the rate of p-hydroxyphenylpyruvate reduction
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r
indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
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r
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3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
indolelactate + NAD+
indolepyruvate + NADH
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r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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involved in aromatic amino acid catabolism
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?
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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involved in aromatic amino acid catabolism
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?
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Mn2+
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required
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0.083
D-phenyllactate
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0.691
indoleglycolate
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0.094 - 1.03
indolelactate
0.076 - 1.77
p-hydroxyphenyllactate
0.044 - 0.075
p-hydroxyphenylpyruvate
0.094
indolelactate
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0.093
NAD+
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0.0077
NADH
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0.076
p-hydroxyphenyllactate
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1.77
p-hydroxyphenyllactate
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0.044
p-hydroxyphenylpyruvate
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0.075
p-hydroxyphenylpyruvate
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6 - 8
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indolepyruvate reduction
8 - 9
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indolelactate oxidation
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brenda
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brenda
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brenda
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E1S7U8_HELP9
Helicobacter pylori (strain 908)
256
0
27907
TrEMBL
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280000
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glycerol density gradient centrifugation
68000
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4 * 68000, SDS-PAGE, gel filtration chromatography
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tetramer
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4 * 68000, SDS-PAGE, gel filtration chromatography
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40
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significant loss of activity above 40°C
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unstable in buffers without glycerol, stabilized by adding 30-50% glycerol to the buffer
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-20°C, 100 mM potassium phosphate, pH 7.5, 1 mM mercaptoethanol, 6 months, no loss of activity, 0°C, 100 mM potassium phosphate, pH 7.5, 1 mM mercaptoethanol, 15 days, no loss of activity
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ammonium sulfate, DEAE-cellulose
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Jean, M.; DeMoss, R.D.
Indolelactate dehydrogenase from Clostridium sporogenes
Can. J. Microbiol.
14
429-435
1968
Clostridium sporogenes
brenda
Bode, R.; Lippoldt, A.; Birnbaum, D.
Purification and properties of D-aromatic lactate dehydrogenase, an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa
Biochem. Physiol. Pflanz.
181
189-198
1986
Candida maltosa
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brenda
Leelayoova, S.; Marbury, D.; Rainey, P.M.; MacKenzie, N.E.; Hall, J.E.
In vitro tryptophan catabolism by Leishmania donovani donovani promastigotes
J. Protozool.
39
350-358
1992
Leishmania donovani donovani
brenda
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1.1.1.110 aromatic 2-oxoacid reductase
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