A0A095AMW7 · MLES_LEUME
- ProteinMalolactic enzyme
- GenemleS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids542 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate.
Catalytic activity
- (S)-malate + H+ = (S)-lactate + CO2
Cofactor
Protein has several cofactor binding sites:
Activity regulation
Oxamate, fructose-1,6-diphosphate and L-lactate act as non-competitive inhibitors, whereas succinate, citrate and tartrate isomers produce a competitive inhibition.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.043 mM | NAD | |||||
16.7 mM | (S)-malate |
pH Dependence
Optimum pH is 4.35.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 92 | Proton donor | ||||
Sequence: Y | ||||||
Active site | 165 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 165 | substrate | ||||
Sequence: K | ||||||
Binding site | 236 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 237 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293-296 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AGTA | ||||||
Binding site | 405 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 450 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 450 | substrate | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | carboxy-lyase activity | |
Molecular Function | malic enzyme activity | |
Molecular Function | malolactic enzyme activity | |
Molecular Function | manganese ion binding | |
Molecular Function | NAD binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Biological Process | malate metabolic process | |
Biological Process | malolactic fermentation | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalolactic enzyme
- EC number
- Short namesMLE
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Leuconostoc
Accessions
- Primary accessionA0A095AMW7
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435672 | 1-542 | Malolactic enzyme | |||
Sequence: MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARNHFYLVDKQGLLFDDTEGLTAAQKPFTRSRKEFVNPEQLINLETIVKELHPTVLIGTSTQPGTFTETIVKSMAENTERPIIFPLSNPTKLAEATAEDLIKWTGGKALVATGIPAADVDYKGVTYKIGQGNNALIYPGLGFGLVASTAKLLTQETISAAIHALGGLVDTDEPGAAVLPPVSNLTDFSQKIAEITAQSVVNQGLNREKIVDPKQAVQDAKWSAEY |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length542
- Mass (Da)59,205
- Last updated2014-11-26 v1
- ChecksumF2B6A27F7E2AA86E