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Information on EC 4.1.1.101 - malolactic enzyme
for references in articles please use BRENDA:EC4.1.1.101
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IUBMB Comments
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 , Lactobacillus plantarum , and Oenococcus oeni [3,4]. The enzyme contains a tightly bound NAD+ cofactor and requires Mn2+.
The enzyme appears in viruses and cellular organisms
- 4.1.1.101
- l-malate
-
wine
- oenococcus
- lactis
- l-lactate
-
lactococcus
- leuconostoc
-
l-malic
- oenos
- grape
- mesenteroides
- plantarum
-
l-lactic
-
winemaking
-
deacidification
- agriculture
-
electrogenic
- food industry
-
transcarbamylase
-
manganese-dependent
-
maepe
-
1.1.1.39
showSynonyms
malolactic enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LEUM_1005
MLE
mleA
mleS
mleA
-
-
-
-
mleS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-malate = (S)-lactate + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: no substrate: D-Malic, DL-tartaric, citric acid, and pyruvic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: D-Malic, DL-tartaric, citric acid, and pyruvic acid
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Fe2+
K+
Mg2+
Mn2+
NH4+
Zn2+
Mn2+
-
allosteric activator, binds to the protein before and independently of malate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
a Saccharomyces cerevisiae peptidic fraction with an apparent molecular masses of 5-10 kDa inhibits the enzyme in synthetic grape juices and in Cabernet Sauvignon and Syrah wines. The peptidic fraction is gradually released during the alcoholic fermentation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
at pH values substantially different from optimum pH 5.5, a positive cooperativity between substrate molecules is observed
-
10.9
L-malate
-
pH 6.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
5.8 - 6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
expression of malolactic enzyme on the cell surface of Saccharomyces cerevisiae. The malolactic activity of the engineered yeast strain can turn 21.11% L-malate into lactic acid after 12 h reaction with L-malate
physiological function
-
heterologous expression in Saccharomyces cerevisiae leads to yeasts producing L-lactate from L-malate, but malate degradation is far from complete. The presence of the mleS gene in Saccharomyces cerevisiae does not influence the viability of cells or the fermentation kinetics. The ethanol yield is normal, and both in wild-type and transformant, L-malate is partially degraded (by 5.6 and 15.6%, respectively)
physiological function
-
inactivation of malolactic enzyme results in higher growth rates and higher final optical densities on L-malate. Limited growth on L-malate of the wild-type strain is correlated to a rapid degradation of the available L-malate to L-lactate, which cannot be further metabolized
physiological function
recombinant Lactobacillus plantarum cells expressing malolactic enzyme accelerate the malolactic fermentation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MLES_LACLA
Lactococcus lactis subsp. lactis (strain IL1403)
540
0
59517
Swiss-Prot
-
MLES_LACPL
Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
547
0
59465
Swiss-Prot
-
A0A644WM46_9ZZZZ
551
0
59738
TrEMBL
other Location (Reliability: 1)
Q03XG6_LEUMM
Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y)
542
0
59075
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
59000
60000
65000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
-
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
-
gene expression is up 250fold increased in the presence of L-malate
optimal conditions for expressions are presence of 7 g/l L-malic acid in the growth medium
gene expression is up 250fold increased in the presence of L-malate
gene expression is up 250fold increased in the presence of L-malate
-
-
optimal conditions for expressions are presence of 7 g/l L-malic acid in the growth medium
-
optimal conditions for expressions are presence of 7 g/l L-malic acid in the growth medium
-
-
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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
LITERATURE
agriculture
food industry
agriculture
-
a Saccharomyces cerevisiae peptidic fraction with an apparent molecular masses of 5-10 kDa inhibits the enzyme in synthetic grape juices and in Cabernet Sauvignon and Syrah wines. The peptidic fraction is gradually released during the alcoholic fermentation
agriculture
comparison of genomes of 10 indigenous Oenococcus oeni strains isolated from Negroamaro wine. All strains possess 10 genes encoding enzymes such as malolactic enzyme (mleA), esterase (estA), citrate lyase (citD, citE and citF), citrate transporter (maeP), a-acetolactate decarboxylase (alsD), aacetolactate synthase (alsS), S-adenosylmethionine synthase (metK) and cystathionine beta-lyase (metC) and result negative in the detection of genes encoding cystathionine gamma-lyase (metB), ornithine transcarbamylase (arcB) and carbamate kinase (arcC)
agriculture
-
isolation of strains for malolactic fermantation. Strain JBE60 shows the highest resistance against 10% (v/v) ethanol and lowers the concentration of malic acid to average 43%
agriculture
-
screening for strains with high malolactic enzyme activites as oenological starter cultures in malolactic fermentation. 2 strains have the capability of growing in wine-like conditions i.e. pH 3.0, ethanol concentration of 14% (v/v) and show malic acid degradation rates of 430.625 mg/l and day and 76.994 mg/l and day, respectively
agriculture
-
isolation of strains for malolactic fermantation. Strain JBE60 shows the highest resistance against 10% (v/v) ethanol and lowers the concentration of malic acid to average 43%
-
agriculture
Oenococcus oeni Vitilactic F
-
a Saccharomyces cerevisiae peptidic fraction with an apparent molecular masses of 5-10 kDa inhibits the enzyme in synthetic grape juices and in Cabernet Sauvignon and Syrah wines. The peptidic fraction is gradually released during the alcoholic fermentation
-
food industry
-
cell surface display of malolactic enzyme on the cell surface of Sacchaormyces cerevisiae to conduct malolactic fermentation in wine. The malolactic activity of the genetically engineered yeast