Detail Information for IndEnz0018001017
IED ID IndEnz0018001017
Enzyme Type ID peroxidase001017
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 Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MQAGKPILYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFTEEFQTLNPMKQVPALKIDGITIVQSLAIMEYLEETRPIPRLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQENQMQWAQKVITSGFNALEKILQSTAGKYCVGDEVSMADVCLVPQVANAERFKVDLSPYPTISHINKELLALEVFQVSHPRRQPDTPAELRT
Enzyme Length 216
Uniprot Accession Number Q9WVL0
Absorption
Active Site
Activity Regulation
Binding Site BINDING 45; /note=Glutathione; /evidence=ECO:0000269|Ref.7; BINDING 59; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|Ref.7; BINDING 111; /note=Glutathione; /evidence=ECO:0000269|Ref.7
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; 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;
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. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
nucleotide Binding
Features Beta strand (5); Binding site (3); Chain (1); Domain (2); Helix (13); Modified residue (6); Region (3); Turn (1)
Keywords 3D-structure;Acetylation;Cytoplasm;Isomerase;Multifunctional enzyme;Phenylalanine catabolism;Phosphoprotein;Reference proteome;Transferase;Tyrosine catabolism
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:O43708; MOD_RES 57; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 136; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:17242355; MOD_RES 137; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 177; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 181; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17242355
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 2CZ2; 2CZ3;
Mapped Pubmed ID 11217851; 12052898; 12466851; 14599561; 14610273; 14651853; 14681479; 15277241; 16278372; 16376852; 18554416; 18799693; 24194600; 27689697; 31267557; 33931597;
Motif
Gene Encoded By
Mass 24,275
Kinetics
Metal Binding
Rhea ID RHEA:14817; RHEA:16437
Cross Reference Brenda