| IED ID | IndEnz0001000042 |
| Enzyme Type ID | amylase000042 |
| Protein Name |
Lactoylglutathione lyase EC 4.4.1.5 Aldoketomutase Allergen Glb33 Glyoxalase I Glx I Glyoxylase I 11 OsGLYI-11 OsGLYI11 Ketone-aldehyde mutase Methylglyoxalase PP33 S-D-lactoylglutathione methylglyoxal lyase allergen Ory s Glyoxalase I |
| Gene Name | GLYI-11 GLX-I Os08g0191700 LOC_Os08g09250 OSJNBa0056O06.9-1 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MASGSEAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDVYKLAEKIKSSCCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ |
| Enzyme Length | 291 |
| Uniprot Accession Number | Q948T6 |
| Absorption | |
| Active Site | ACT_SITE 96; /evidence=ECO:0000305|PubMed:24661284; ACT_SITE 145; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:24661284; ACT_SITE 158; /evidence=ECO:0000305|PubMed:24661284; ACT_SITE 209; /evidence=ECO:0000305|PubMed:24661284 |
| Activity Regulation | |
| Binding Site | BINDING 31; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04760; BINDING 82; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04760; BINDING 96; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04760 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:11139585}; |
| DNA Binding | |
| EC Number | 4.4.1.5 |
| Enzyme Function | FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (By similarity). Involved in the detoxifiation of methylglyoxal. Can functionally complement growth defect of a yeast mutant lacking GLY I. Involved in abiotic stress response. Over-expression of GLYI-11 in tobacco increases tolerance to osmotic, oxidative and salt stresses (PubMed:24661284). {ECO:0000250|UniProtKB:Q04760, ECO:0000269|PubMed:24661284}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:24661284}; |
| Pathway | PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Active site (4); Binding site (3); Chain (1); Domain (2); Metal binding (2); Mutagenesis (3); Sequence conflict (1) |
| Keywords | Allergen;Direct protein sequencing;Lyase;Metal-binding;Nickel;Phosphoprotein;Reference proteome;Repeat |
| Interact With | |
| Induction | INDUCTION: By salt stress and hydrogen peroxide (PubMed:21213008). Induced by methylglyoxal (PubMed:24661284). {ECO:0000269|PubMed:21213008, ECO:0000269|PubMed:24661284}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Phosphorylated after gibberellin treatment. {ECO:0000269|PubMed:16028114}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,553 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.6 mM for methylglyoxal {ECO:0000269|PubMed:11139585}; KM=99.8 uM for glutatione {ECO:0000269|PubMed:24661284}; Vmax=130.8 umol/min/mg enzyme with glutatione as substrate {ECO:0000269|PubMed:24661284}; |
| Metal Binding | METAL 145; /note=Nickel; /evidence=ECO:0000305|PubMed:24661284; METAL 209; /note=Nickel; /evidence=ECO:0000305|PubMed:24661284 |
| Rhea ID | RHEA:19069 |
| Cross Reference Brenda | 4.4.1.5; |