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Literature summary 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

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.345 0.14
-
NADH at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 0.21
-
3-methyl-2-oxopentanoate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 0.21
-
2-oxomethylvalerate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 0.29
-
3-methyl-2-oxobutanoate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 0.29
-
2-oxoisovalerate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 0.3
-
4-methyl-2-oxopentanoate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 0.3
-
2-oxoisocaproate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 0.53
-
2-oxovalerate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 1.26
-
2-formylbutanethioate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 1.26
-
4-methylthio-2-oxobutanoate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 1.5
-
benzoylformate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 1.5
-
benzoylformate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 2.4
-
2-oxocaproate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 3
-
D-mandelate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 3
-
DL-2-hydroxyisocaproate at pH 7.0 and 37°C Lactococcus lactis
1.1.1.345 5.4
-
phenylpyruvate pH 7.0, 37°C Lactococcus cremoris
1.1.1.345 5.4
-
phenylpyruvate at pH 7.0 and 37°C Lactococcus lactis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.345 34361
-
2 * 34361, calculated from amino acid sequence Lactococcus lactis
1.1.1.345 36000
-
2 * 36000, SDS-PAGE Lactococcus cremoris
1.1.1.345 36000
-
2 * 36000, His-tagged fusion protein, SDS-PAGE Lactococcus lactis
1.1.1.345 70000
-
gel filtration Lactococcus lactis
1.1.1.345 70000
-
gel filtration Lactococcus cremoris

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.345 Lactococcus cremoris
-
-
-
1.1.1.345 Lactococcus cremoris TIL46
-
-
-
1.1.1.345 Lactococcus lactis
-
-
-
1.1.1.345 Lactococcus lactis IL1403
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.345
-
Lactococcus cremoris

Storage Stability

EC Number Storage Stability Organism
1.1.1.345 4°C, concentrated enzyme solution at pH 7.0 (10.6 mg/ml), 3 months, without significant loss of activity Lactococcus lactis
1.1.1.345 4°C, diluted enzyme solution at pH 7.0 (0.004 mg/ml), 1 h, 40% loss of activity Lactococcus lactis
1.1.1.345 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.345 2-formylbutanethioate + NADH + H+ i.e. 2-ketomethylthiobutyrate Lactococcus cremoris ?
-
?
1.1.1.345 2-formylbutanethioate + NADH + H+ i.e. 2-ketomethylthiobutyrate Lactococcus cremoris TIL46 ?
-
?
1.1.1.345 2-oxobutyrate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxobutyrate + NADH + H+
-
Lactococcus lactis IL1403 ? + NAD+
-
r
1.1.1.345 2-oxocaproate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxocaproate + NADH + H+
-
Lactococcus lactis IL1403 ? + NAD+
-
r
1.1.1.345 2-oxoisocaproate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxoisocaproate + NADH + H+
-
Lactococcus lactis IL1403 ? + NAD+
-
r
1.1.1.345 2-oxoisovalerate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxomethylthiobutyrate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxomethylvalerate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 2-oxovalerate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 3-methyl-2-oxobutanoate + NADH + H+ i.e.2-oxoisovalerate Lactococcus cremoris 2-hydroxy-3-methylbutanoate + NAD+
-
?
1.1.1.345 3-methyl-2-oxobutanoate + NADH + H+ i.e.2-oxoisovalerate Lactococcus cremoris TIL46 2-hydroxy-3-methylbutanoate + NAD+
-
?
1.1.1.345 3-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxomethylvalerate Lactococcus cremoris 2-hydroxy-3-methylpentanoate + NAD+
-
?
1.1.1.345 3-methyl-2-oxopentanoate + NADH + H+ i.e. 2-oxomethylvalerate Lactococcus cremoris TIL46 2-hydroxy-3-methylpentanoate + NAD+
-
?
1.1.1.345 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
1.1.1.345 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
1.1.1.345 benzoylformate + NADH + H+
-
Lactococcus cremoris ?
-
?
1.1.1.345 benzoylformate + NADH + H+
-
Lactococcus cremoris TIL46 ?
-
?
1.1.1.345 benzoylformate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 D-mandelate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 DL-2-hydroxyisocaproate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 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 ?
-
?
1.1.1.345 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 ?
-
?
1.1.1.345 phenylpyruvate + NADH + H+
-
Lactococcus lactis ? + NAD+
-
r
1.1.1.345 phenylpyruvate + NADH + H+
-
Lactococcus lactis IL1403 ? + NAD+
-
r
1.1.1.345 phenylpyruvate + NADH + H+
-
Lactococcus cremoris phenyllactate + NAD+
-
?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.345 37
-
assay at Lactococcus cremoris
1.1.1.345 55
-
-
Lactococcus lactis
1.1.1.345 55
-
-
Lactococcus cremoris

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.345 37 55 at 37°C, the activity reaches about 65% of peak activity at 55°C Lactococcus lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.345 5.5 7 forward reaction Lactococcus lactis
1.1.1.345 7
-
assay at Lactococcus cremoris
1.1.1.345 9
-
reverse reaction Lactococcus lactis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.345 5 8 activity is reduced by only about 10% at pH 5.0 and 8.0 Lactococcus lactis
1.1.1.345 5.5 7 reduction of 4-methyl-2-oxopentanoate Lactococcus cremoris
1.1.1.345 9
-
oxidation of (R)-2-hydroxy-4-methylpentanoate Lactococcus cremoris

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.345 5 8 activity is reduced by about 10% at pH 5.0 and 8.0 Lactococcus cremoris

Cofactor

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

General Information

EC Number General Information Comment Organism
1.1.1.345 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
1.1.1.345 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
1.1.1.345 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