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Literature summary for 1.1.1.110 extracted from

  • 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 (1986), Biochem. Physiol. Pflanz., 181, 189-198.
No PubMed abstract available

General Stability

General Stability Organism
unstable in buffers without glycerol, stabilized by adding 30-50% glycerol to the buffer Candida maltosa

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Candida maltosa
EDTA
-
Candida maltosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0077
-
NADH
-
Candida maltosa
0.0086
-
NADPH
-
Candida maltosa
0.021
-
NADP+
-
Candida maltosa
0.044
-
p-hydroxyphenylpyruvate
-
Candida maltosa
0.067
-
Indolepyruvate
-
Candida maltosa
0.076
-
p-hydroxyphenyllactate
-
Candida maltosa
0.083
-
D-phenyllactate
-
Candida maltosa
0.093
-
NAD+
-
Candida maltosa
0.094
-
indolelactate
-
Candida maltosa

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ inhibitory Candida maltosa
Mn2+ required Candida maltosa
Zn2+ inhibitory Candida maltosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
68000
-
4 * 68000, SDS-PAGE, gel filtration chromatography Candida maltosa
250000
-
gel filtration Candida maltosa
280000
-
glycerol density gradient centrifugation Candida maltosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-(4-hydroxyphenyl)pyruvate + NAD(P)H Candida maltosa involved in aromatic amino acid catabolism (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Candida maltosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Candida maltosa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.5
-
crude extract Candida maltosa
1170
-
purified enzyme Candida maltosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-ketoisopentanoate + NAD(P)H poor substrate Candida maltosa 2-hydroxyisopentanoate + NAD(P)+
-
r
2-oxobutyrate + NAD(P)H + H+ poor substrate Candida maltosa 2-hydroxybutyrate + NAD(P)+
-
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H the initial rate of oxidation is 100 fold lower than that of reduction Candida maltosa (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
-
r
3-(4-hydroxyphenyl)pyruvate + NAD(P)H involved in aromatic amino acid catabolism Candida maltosa (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+
-
?
indolepyruvate + NAD(P)H reduction at 30% the rate of p-hydroxyphenylpyruvate reduction Candida maltosa indolelactate + NAD(P)+
-
r
additional information best substrate for oxidation is p-hydroxyphenyllactate, D-phenyllactate is oxidized at 75% and indolelactate at 52% the rate of p-hydroxyphenyllactate Candida maltosa ?
-
?
phenylpyruvate + NAD(P)H reduction at 27% the rate of p-hydroxyphenylpyruvate reduction Candida maltosa D-phenyllactate + NAD(P)+
-
r
pyruvate + NAD(P)H + H+ poor substrate Candida maltosa lactate + NAD(P)+
-
r

Subunits

Subunits Comment Organism
tetramer 4 * 68000, SDS-PAGE, gel filtration chromatography Candida maltosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Candida maltosa

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60
-
Candida maltosa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
significant loss of activity above 40°C Candida maltosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
reduction Candida maltosa
9.5
-
oxidation Candida maltosa