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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, EC 1.1.1.222, indolelactate dehydrogenase, more
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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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EC 1.1.1.222
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formerly
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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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MetaCyc
4-hydroxybenzoate biosynthesis I (eukaryotes), L-phenylalanine degradation IV (mammalian, via side chain), L-phenylalanine degradation VI (reductive Stickland reaction), L-tryptophan degradation IV (via indole-3-lactate), L-tryptophan degradation XIII (reductive Stickland reaction), L-tyrosine degradation V (reductive Stickland reaction), tropane alkaloids biosynthesis
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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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Substrates: poor substrate Products: -
r
2-oxobutyrate + NAD(P)H + H+
2-hydroxybutyrate + NAD(P)+
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Substrates: poor substrate Products: -
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
indoleglycolate + NAD+
indoleglyoxylate + NADH
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Substrates: - Products: -
r
indolelactate + NAD+
indolepyruvate + NADH
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Substrates: - Products: -
r
indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
p-hydroxyphenyllactate + NAD+
p-hydroxyphenylpyruvate + NADH
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Substrates: - Products: -
r
phenyllactate + NAD+
phenylpyruvate + NADH
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Substrates: - Products: -
r
phenylpyruvate + NAD(P)H
D-phenyllactate + NAD(P)+
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Substrates: reduction at 27% the rate of p-hydroxyphenylpyruvate reduction Products: -
r
pyruvate + NAD(P)H + H+
lactate + NAD(P)+
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Substrates: poor substrate Products: -
r
additional information
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Substrates: best substrate for oxidation is p-hydroxyphenyllactate, D-phenyllactate is oxidized at 75% and indolelactate at 52% the rate of p-hydroxyphenyllactate Products: -
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3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: the initial rate of oxidation is 100 fold lower than that of reduction Products: -
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: involved in aromatic amino acid catabolism Products: -
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3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: - Products: -
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: involved in aromatic amino acid catabolism Products: -
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indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
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Substrates: reduction at 30% the rate of p-hydroxyphenylpyruvate reduction Products: -
r
indolepyruvate + NAD(P)H
indolelactate + NAD(P)+
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Substrates: - Products: -
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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Substrates: - Products: -
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: involved in aromatic amino acid catabolism Products: -
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3-(4-hydroxyphenyl)pyruvate + NAD(P)H
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
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Substrates: involved in aromatic amino acid catabolism Products: -
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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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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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FLDH_CLOS1
Clostridium sporogenes (strain ATCC 15579)
331
0
36592
Swiss-Prot
other Location (Reliability: 2 )
FLDH_CLOS3
Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB 8053 / NCTC 8594 / PA 3679)
331
0
36507
Swiss-Prot
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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
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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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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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