MLES_OENOE
ID MLES_OENOE Reviewed; 541 AA.
AC Q48796; D0EZL3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Malolactic enzyme {ECO:0000303|PubMed:8919788};
DE Short=MLE {ECO:0000303|PubMed:8919788};
DE EC=4.1.1.101 {ECO:0000269|PubMed:2097345, ECO:0000269|PubMed:22452826, ECO:0000269|PubMed:23196745};
GN Name=mleA {ECO:0000303|PubMed:8919788};
OS Oenococcus oeni (Leuconostoc oenos).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=1247;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=8413;
RX PubMed=8919788; DOI=10.1128/aem.62.4.1274-1282.1996;
RA Labarre C., Guzzo J., Cavin J.F., Divies C.;
RT "Cloning and characterization of the genes encoding the malolactic enzyme
RT and the malate permease of Leuconostoc oenos.";
RL Appl. Environ. Microbiol. 62:1274-1282(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=DSM 20255;
RX PubMed=22452826; DOI=10.1186/2191-0855-2-19;
RA Schumann C., Michlmayr H., Eder R., Del Hierro A.M., Kulbe K.D.,
RA Mathiesen G., Nguyen T.H.;
RT "Heterologous expression of Oenococcus oeni malolactic enzyme in
RT Lactobacillus plantarum for improved malolactic fermentation.";
RL AMB Express 2:19-19(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 23278;
RX PubMed=2097345; DOI=10.1002/jobm.3620300813;
RA Naouri P., Chagnaud P., Arnaud A., Galzy P.;
RT "Purification and properties of a malolactic enzyme from Leuconostoc oenos
RT ATCC 23278.";
RL J. Basic Microbiol. 30:577-585(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 20255;
RX PubMed=23196745; DOI=10.4161/bioe.22988;
RA Schuemann C., Michlmayr H., Del Hierro A.M., Kulbe K.D., Jiranek V.,
RA Eder R., Nguyen T.H.;
RT "Malolactic enzyme from Oenococcus oeni: heterologous expression in
RT Escherichia coli and biochemical characterization.";
RL Bioengineered 4:147-152(2013).
CC -!- FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which
CC results in a natural decrease in acidity and favorable changes in wine
CC flavors. Catalyzes the decarboxylation of L-malate to L-lactate. It can
CC also use pyruvate as substrate. {ECO:0000269|PubMed:2097345,
CC ECO:0000269|PubMed:22452826, ECO:0000269|PubMed:23196745,
CC ECO:0000269|PubMed:8919788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16651; EC=4.1.1.101;
CC Evidence={ECO:0000269|PubMed:2097345, ECO:0000269|PubMed:22452826,
CC ECO:0000269|PubMed:23196745};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:2097345, ECO:0000269|PubMed:22452826,
CC ECO:0000269|PubMed:23196745};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:2097345, ECO:0000269|PubMed:22452826,
CC ECO:0000269|PubMed:23196745};
CC -!- ACTIVITY REGULATION: L-lactate and ethanol are non-competitive
CC inhibitors, whereas succinate, citrate, and D-tartrate show competitive
CC type inhibitions. {ECO:0000269|PubMed:2097345}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0054 mM for manganese {ECO:0000269|PubMed:23196745};
CC KM=0.017 mM for manganese {ECO:0000269|PubMed:2097345};
CC KM=0.082 mM for NAD {ECO:0000269|PubMed:23196745};
CC KM=0.044 mM for NAD {ECO:0000269|PubMed:2097345};
CC KM=5.3 mM for (S)-malate {ECO:0000269|PubMed:23196745};
CC KM=17 mM for (S)-malate {ECO:0000269|PubMed:2097345};
CC Vmax=175 umol/min/mg enzyme toward manganese
CC {ECO:0000269|PubMed:23196745};
CC Vmax=213 umol/min/mg enzyme toward NAD {ECO:0000269|PubMed:23196745};
CC Vmax=219 umol/min/mg enzyme toward (S)-malate
CC {ECO:0000269|PubMed:23196745};
CC Note=kcat is 187 sec(-1) with manganese as substrate. kcat is 227
CC sec(-1) with NAD as substrate. kcat is 234 sec(-1) with (S)-malate as
CC substrate. {ECO:0000269|PubMed:23196745};
CC pH dependence:
CC Optimum pH is between 5 and 6. {ECO:0000269|PubMed:2097345,
CC ECO:0000269|PubMed:22452826, ECO:0000269|PubMed:23196745};
CC Temperature dependence:
CC Optimum temperature is between 37 and 45 degrees Celsius.
CC {ECO:0000269|PubMed:2097345, ECO:0000269|PubMed:22452826,
CC ECO:0000269|PubMed:23196745};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2097345,
CC ECO:0000269|PubMed:23196745}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; X82326; CAA57769.1; -; Genomic_DNA.
DR EMBL; GQ924754; ACX50963.1; -; Genomic_DNA.
DR PIR; T13496; T13496.
DR RefSeq; WP_002817634.1; NZ_MLOM01000319.1.
DR AlphaFoldDB; Q48796; -.
DR SMR; Q48796; -.
DR GeneID; 57296176; -.
DR KEGG; ag:ACX50963; -.
DR BioCyc; MetaCyc:MON-19375; -.
DR BRENDA; 4.1.1.101; 3009.
DR SABIO-RK; Q48796; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0043464; P:malolactic fermentation; IDA:UniProtKB.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Lyase; Manganese; Metal-binding; NAD.
FT CHAIN 1..541
FT /note="Malolactic enzyme"
FT /id="PRO_0000160250"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 292..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 449
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT CONFLICT 2
FT /note="T -> I (in Ref. 2; ACX50963)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="A -> V (in Ref. 2; ACX50963)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="D -> E (in Ref. 2; ACX50963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59118 MW; 7D6AAEE223273AFE CRC64;
MTDPVSILND PFINKGTAFT EAEREELGLN GLLPAKVQAL QEQVDQTYAQ FQSKVSNLEK
RLFLMEIFNT NHVLFYKLFS QHVVEFMPIV YDPTIADTIE NYSELFVEPQ GAAFLDINHP
ENIQSTLKNA ANGRDIKLLV VSDAEGILGI GDWGVQGVDI AVGKLMVYTV AAGIDPSTVL
AVVIDAGTNN EKLLKDPMYL GNKFNRVRGD KYYDFIDKFV NHAESLFPNL YLHWEDFGRS
NASNILNSYK DKIATFNDDI QGTGIVVLAG VLGALKISGQ KLTDQTYMSF GAGTAGMGIV
KQLHEEMVEQ GLSDEEAKKH FFLVDKQGLL FDDDPDLTPE QKPFAAKRSD FKNANQLTNL
QAAVEAVHPT ILVGTSTHPN SFTEEIVKDM SGYTERPIIF PISNPTKLAE AKAEDVLKWS
NGKALIGTGV PVDDIEYEGN AYQIGQANNA LIYPGLGFGA IAAQSKLLTP EMISAAAHSL
GGIVDTTKVG AAVLPPVSKL ADFSRTVAVA VAKKAVEQGL NRQPIDDVEK AVDDLKWDPK
Y
