Q12320 · GLO4_YEAST
- ProteinHydroxyacylglutathione hydrolase, mitochondrial
- GeneGLO4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids285 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thiolesterase that catalyzes the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. Involved in the metabolism of methylglyoxal, a toxic compound for yeast proliferation, by converting methylglyoxal to lactate via S-D-lactoylglutathione by sequential enzyme reactions catalyzed by glyoxalase I and glyoxalase II.
Catalytic activity
- an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H+
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Inhibited by various thiol compounds such as glutathione and coenzyme A.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
79.3 μM | (R)-S-lactoylglutathione | |||||
25.6 μM | (R)-S-mandeloylglutathione |
kcat is 605 sec-1 with (R)-S-lactoylglutathione as substrate and 38.1 sec-1 with (R)-S-mandeloylglutathione as substrate.
pH Dependence
Optimum pH is 6.5-9.
Pathway
Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 69 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 71 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 73 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 74 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 131 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 154 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 154 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 198 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | hydroxyacylglutathione hydrolase activity | |
Molecular Function | metal ion binding | |
Biological Process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydroxyacylglutathione hydrolase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ12320
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-10 | Mitochondrion | |||
Chain | PRO_0000012285 | 11-285 | Hydroxyacylglutathione hydrolase, mitochondrial | ||
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length285
- Mass (Da)32,339
- Last updated1996-11-01 v1
- Checksum09DF2E4B5B9C0E52
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X82893 EMBL· GenBank· DDBJ | CAA58065.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X87331 EMBL· GenBank· DDBJ | CAA60759.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74948 EMBL· GenBank· DDBJ | CAA99230.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692965 EMBL· GenBank· DDBJ | AAT92984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA10823.1 EMBL· GenBank· DDBJ | Genomic DNA |