| IED ID | IndEnz0018000842 |
| Enzyme Type ID | peroxidase000842 |
| Protein Name |
Maleylacetoacetate isomerase MAAI EC 5.2.1.2 GSTZ1-1 Glutathione S-transferase zeta 1 EC 2.5.1.18 |
| Gene Name | Gstz1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MQAGKPVLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPRLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTPAELRT |
| Enzyme Length | 216 |
| Uniprot Accession Number | P57113 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 45; /note=Glutathione; /evidence=ECO:0000250; BINDING 59; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250; BINDING 111; /note=Glutathione; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4-maleylacetoacetate = 4-fumarylacetoacetate; Xref=Rhea:RHEA:14817, ChEBI:CHEBI:17105, ChEBI:CHEBI:18034; EC=5.2.1.2; Evidence={ECO:0000269|PubMed:9531472}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:9531472}; |
| DNA Binding | |
| EC Number | 5.2.1.2; 2.5.1.18 |
| Enzyme Function | FUNCTION: Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumene hydroperoxides (By similarity). Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. {ECO:0000250, ECO:0000269|PubMed:9531472}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6. |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Domain (2); Modified residue (6); Region (3) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Isomerase;Multifunctional enzyme;Phenylalanine catabolism;Phosphoprotein;Reference proteome;Transferase;Tyrosine catabolism |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9531472}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:O43708; MOD_RES 57; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9WVL0; MOD_RES 136; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9WVL0; MOD_RES 137; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 177; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9WVL0; MOD_RES 181; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,961 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=71.4 uM for dichloroacetic acid {ECO:0000269|PubMed:9531472}; KM=59.0 uM for glutathione {ECO:0000269|PubMed:9531472}; Vmax=1334 nmol/min/mg enzyme {ECO:0000269|PubMed:9531472}; |
| Metal Binding | |
| Rhea ID | RHEA:14817; RHEA:16437 |
| Cross Reference Brenda |