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Literature summary for 1.1.1.345 extracted from

  • Chambellon, E.; Rijnen, L.; Lorquet, F.; Gitton, C.; Van Hylckama Vlieg, J.; Wouters, J.; Yvon, M.
    The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis (2009), J. Bacteriol., 191, 873-881.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.345

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 154% activity at 20 mM Lactococcus lactis
dithiothreitol 20 mM, 1.5fold activation Lactococcus cremoris
EDTA 160% activity at 10 mM Lactococcus lactis
EDTA 10 mM, 1.6fold activation Lactococcus cremoris

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta cells Lactococcus lactis
overexpression in Escherichia coli as His-tagged fusion protein Lactococcus cremoris

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 72% residual activity at 1 mM Lactococcus lactis
CaCl2 1 mM, 28% inhibition Lactococcus cremoris
Cu2+ complete inhibition at 0.1 mM Lactococcus lactis
CuSO4 0.1 mM, complete inhibition Lactococcus cremoris
DEPC 65% residual activity at 1 mM, 12% residual activity at 2 mM Lactococcus lactis
diethyl dicarbonate 2 mM, 88% inhibition Lactococcus cremoris
Hg2+ complete inhibition at 0.1 mM Lactococcus lactis
HgCl2 0.1 mM, complete inhibition Lactococcus cremoris
iodoacetamide 0.1 mM, 5% inhibition Lactococcus cremoris
iodoacetamide 95% residual activity at 1 mM Lactococcus lactis
Mg2+ 83% residual activity at 1 mM Lactococcus lactis
MgCl2 1 mM, 17% inhibition Lactococcus cremoris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
 NADH at pH 7.0 and 37°C Lactococcus lactis
0.21
-
 3-methyl-2-oxopentanoate pH 7.0, 37°C Lactococcus cremoris
0.21
-
 2-oxomethylvalerate at pH 7.0 and 37°C Lactococcus lactis
0.29
-
 3-methyl-2-oxobutanoate pH 7.0, 37°C Lactococcus cremoris
0.29
-
 2-oxoisovalerate at pH 7.0 and 37°C Lactococcus lactis
0.3
-
 4-methyl-2-oxopentanoate pH 7.0, 37°C Lactococcus cremoris
0.3
-
 2-oxoisocaproate at pH 7.0 and 37°C Lactococcus lactis
0.53
-
 2-oxovalerate at pH 7.0 and 37°C Lactococcus lactis
1.26
-
 2-formylbutanethioate pH 7.0, 37°C Lactococcus cremoris
1.26
-
 4-methylthio-2-oxobutanoate at pH 7.0 and 37°C Lactococcus lactis
1.5
-
 benzoylformate pH 7.0, 37°C Lactococcus cremoris
1.5
-
 benzoylformate at pH 7.0 and 37°C Lactococcus lactis
2.4
-
 2-oxocaproate at pH 7.0 and 37°C Lactococcus lactis
3
-
 D-mandelate at pH 7.0 and 37°C Lactococcus lactis
3
-
 DL-2-hydroxyisocaproate at pH 7.0 and 37°C Lactococcus lactis
5.4
-
 phenylpyruvate pH 7.0, 37°C Lactococcus cremoris
5.4
-
 phenylpyruvate at pH 7.0 and 37°C Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34361
-
 2 * 34361, calculated from amino acid sequence Lactococcus lactis
36000
-
 2 * 36000, SDS-PAGE Lactococcus cremoris
36000
-
 2 * 36000, His-tagged fusion protein, SDS-PAGE Lactococcus lactis
70000
-
 gel filtration Lactococcus lactis
70000
-
 gel filtration Lactococcus cremoris

Organism

Organism UniProt Comment Textmining
Lactococcus cremoris
-
-
-
Lactococcus cremoris TIL46
-
-
-
Lactococcus lactis
-
-
-
Lactococcus lactis IL1403
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Lactococcus cremoris

Storage Stability

Storage Stability Organism
4°C, concentrated enzyme solution at pH 7.0 (10.6 mg/ml), 3 months, without significant loss of activity Lactococcus lactis
4°C, diluted enzyme solution at pH 7.0 (0.004 mg/ml), 1 h, 40% loss of activity Lactococcus lactis
4°C, pH 7.0, concentrated enzyme solution (10.6 mg/ml) is stable for at least 2-3 months Lactococcus cremoris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-formylbutanethioate + NADH + H+ i.e. 2-ketomethylthiobutyrate Lactococcus cremoris ?
-
 ?
2-formylbutanethioate + NADH + H+ i.e. 2-ketomethylthiobutyrate Lactococcus cremoris TIL46 ?
-
 ?
2-oxobutyrate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxobutyrate + NADH + H+
-
 Lactococcus lactis IL1403 ? + NAD+
-
 r
2-oxocaproate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxocaproate + NADH + H+
-
 Lactococcus lactis IL1403 ? + NAD+
-
 r
2-oxoisocaproate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxoisocaproate + NADH + H+
-
 Lactococcus lactis IL1403 ? + NAD+
-
 r
2-oxoisovalerate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxomethylthiobutyrate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxomethylvalerate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
2-oxovalerate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
3-methyl-2-oxobutanoate + NADH + H+ i.e.2-oxoisovalerate Lactococcus cremoris 2-hydroxy-3-methylbutanoate + NAD+
-
 ?
3-methyl-2-oxobutanoate + NADH + H+ i.e.2-oxoisovalerate Lactococcus cremoris TIL46 2-hydroxy-3-methylbutanoate + NAD+
-
 ?
3-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxomethylvalerate Lactococcus cremoris 2-hydroxy-3-methylpentanoate + NAD+
-
 ?
3-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxomethylvalerate Lactococcus cremoris TIL46 2-hydroxy-3-methylpentanoate + NAD+
-
 ?
4-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction Lactococcus cremoris (R)-2-hydroxy-4-methylpentanoate + NAD+ i.e. (R)-2-hydroxyisocaproate r
4-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction Lactococcus cremoris TIL46 (R)-2-hydroxy-4-methylpentanoate + NAD+ i.e. (R)-2-hydroxyisocaproate r
benzoylformate + NADH + H+
-
 Lactococcus cremoris ?
-
 ?
benzoylformate + NADH + H+
-
 Lactococcus cremoris TIL46 ?
-
 ?
benzoylformate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
D-mandelate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
DL-2-hydroxyisocaproate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
additional information the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH Lactococcus lactis ?
-
 ?
additional information the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH Lactococcus lactis IL1403 ?
-
 ?
phenylpyruvate + NADH + H+
-
 Lactococcus lactis ? + NAD+
-
 r
phenylpyruvate + NADH + H+
-
 Lactococcus lactis IL1403 ? + NAD+
-
 r
phenylpyruvate + NADH + H+
-
 Lactococcus cremoris phenyllactate + NAD+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 36000, SDS-PAGE Lactococcus cremoris
homodimer 2 * 34361, calculated from amino acid sequence Lactococcus lactis
homodimer 2 * 36000, His-tagged fusion protein, SDS-PAGE Lactococcus lactis

Synonyms

Synonyms Comment Organism
D-2-hydroxyacid dehydrogenase
-
 Lactococcus lactis
D-HicDH
-
 Lactococcus lactis
HdhD
-
 Lactococcus cremoris
PanE
-
 Lactococcus lactis
PanE formerly Lactococcus cremoris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Lactococcus cremoris
55
-
-
 Lactococcus lactis
55
-
-
 Lactococcus cremoris

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 55 at 37°C, the activity reaches about 65% of peak activity at 55°C Lactococcus lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 7 forward reaction Lactococcus lactis
7
-
 assay at Lactococcus cremoris
9
-
 reverse reaction Lactococcus lactis

pH Range

pH Minimum pH Maximum Comment Organism
5 8 activity is reduced by only about 10% at pH 5.0 and 8.0 Lactococcus lactis
5.5 7 reduction of 4-methyl-2-oxopentanoate Lactococcus cremoris
9
-
 oxidation of (R)-2-hydroxy-4-methylpentanoate Lactococcus cremoris

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 activity is reduced by about 10% at pH 5.0 and 8.0 Lactococcus cremoris

Cofactor

Cofactor Comment Organism Structure
NADH NADH is the exclusive coenzyme Lactococcus lactis
NADH NADPH shows no activity as cosubstrate Lactococcus cremoris

General Information

General Information Comment Organism
malfunction the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate Lactococcus lactis
malfunction the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate Lactococcus cremoris
metabolism its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine Lactococcus cremoris