| IED ID | IndEnz0018001016 |
| Enzyme Type ID | peroxidase001016 |
| 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 MAAI |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA |
| Enzyme Length | 216 |
| Uniprot Accession Number | O43708 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 45; /note=Glutathione; /evidence=ECO:0000269|PubMed:11327815; BINDING 59; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:11327815; BINDING 111; /note=Glutathione; /evidence=ECO:0000269|PubMed:11327815 |
| 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:10739172}; 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:10739172}; |
| DNA Binding | |
| EC Number | 5.2.1.2; 2.5.1.18 |
| Enzyme Function | FUNCTION: 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. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. {ECO:0000269|PubMed:10739172}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6. |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (5); Binding site (3); Chain (1); Domain (2); Helix (12); Modified residue (5); Natural variant (7); Region (3); Turn (1) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Disease variant;Isomerase;Multifunctional enzyme;Phenylalanine catabolism;Phosphoprotein;Reference proteome;Transferase;Tyrosine catabolism |
| Interact With | Q5SYC1; Q9H8Y8; Itself; P16333; Q58EX7; P47897; Q8WWU5-7; Q12933; Q9H0C1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:22814378; MOD_RES 32; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 57; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9WVL0; MOD_RES 136; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9WVL0; MOD_RES 177; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9WVL0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1FW1; |
| Mapped Pubmed ID | 10329152; 10587441; 10783391; 11737895; 12042665; 12211029; 12627223; 16081649; 16189514; 16298388; 16548513; 17474147; 17601350; 18977241; 19859803; 20083122; 20085333; 20884751; 21106529; 21382349; 21668448; 22522127; 25416956; 8182750; 8203914; 8331657; 8431482; 9551553; 9710704; 9839448; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,212 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14817; RHEA:16437 |
| Cross Reference Brenda | 2.5.1.18;5.2.1.2; |