Information on EC 4.1.1.101 - malolactic enzyme

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.101
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RECOMMENDED NAME
GeneOntology No.
malolactic enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-malate = (S)-lactate + CO2
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-malate degradation I
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate carboxy-lyase
The enzyme is involved in the malolactic fermentation of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. It has been purified from several lactic acid bacteria, including Leuconostoc mesenteroides [1], Lactobacillus plantarum [2], and Oenococcus oeni [3,4]. The enzyme contains a tightly bound NAD+ cofactor and requires Mn2+.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate
(S)-lactate + CO2
show the reaction diagram
D-malate
D-lactate + CO2
show the reaction diagram
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-
-
-
?
DL-malate
DL-lactate + CO2
show the reaction diagram
-
-
-
-
?
L-malate
L-lactate + CO2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
about 20% of the activity with Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
D-fructose-1,6-bisphosphate
-
noncompetitive
D-Tartrate
dithiothreitol
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0.1 mM, 44% residual activity
EDTA
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0.1 mM, no residual activity
ethanol
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competitive
L-lactate
L-Tartrate
-
competitive
meso-tartrate
-
competitive
N-bromosuccinimide
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0.1 mM, 31% residual activity
oxamate
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noncompetitive
succinate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 12.5
(S)-malate
8.3
D-malate
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pH 4.5, 25°C, activity of cell extract
8
DL-malate
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pH 4.5, 25°C, activity of cell extract
2.8 - 17
L-malate
additional information
additional information
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at pH values substantially different from optimum pH 5.5, a positive cooperativity between substrate molecules is observed
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000011
citrate
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pH 6.0, 25°C
32
D-fructose-1,6-bisphosphate
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pH 6.0, 25°C
11
D-Tartrate
-
pH 6.0, 25°C
276
L-lactate
-
pH 6.0, 25°C
1.2
L-Tartrate
-
pH 6.0, 25°C
10
meso-tartrate
-
pH 6.0, 25°C
9
oxamate
-
pH 6.0, 25°C
78
succinate
-
pH 6.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16.23
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pH 6.0, 25°C
265
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pH 6.0, 37°C
419.2
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pH 6.0, 30°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
72% of maximum activity
45
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50% residual activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
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isoelectric focusing
4.35
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isoelectric focusing
4.4
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isoelectric focusing
4.8
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calculated
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59118
x * 59118, calculated
59534
x * 59534, calculated
62300
x * 62300, calculated, x * 60000, SDS-PAGE
66000
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2 * 66000, SDS-PAGE
70000
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2 * 70000, SDS-PAGE
110000
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2 * 110000, SDS-PAGE
130000
132000
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gel filtration
220000
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gel filtration
235000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, presence of 0.1 M NaCl, half-life 30 days
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is constitutively expressed. Addition of L-malic acid (37 mM) to the growth medium results in increased activity, addition of the D-isomer alone or the racemic mixture results in lower activities. Addition of the main sugars in apple juice (fructose, sucrose, and glucose) to the growth medium in the presence of malic acid represses production of the enzyme. In the absence of malic acid, addition of sugars to the growth medium somewhat increases the residual malolactic activity
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expression of malolactic enzyme is decreased in the presence of ethanol
expression of malolactic enzyme is inducible by the presence of malic acid, with increased expression in the middle of malolactic fermentation. Expression is also increased at low pH values
expression of mle genes encoding malolactic enzyme mleS, the putative L-malate transporter MleT, and the putative regulator MleR is induced by L-malic acid and it is not subject to carbon catabolite repression
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optimal conditions for expressions are presence of 7 g/l L-malic acid in the growth medium
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
presence of NAD+ protects against inactivation. Additiion of NAD+, after dissociation, restores malolactic activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry