IED Industry Enzyme Database

Detail Information for IndEnz0018001087
IED ID IndEnz0018001087
Enzyme Type ID peroxidase001087
Protein Name Heme oxygenase 1
HO-1
EC 1.14.14.18

Cleaved into: Heme oxygenase 1 soluble form
Gene Name HMOX1 HO HO1
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 MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Enzyme Length 288
Uniprot Accession Number P09601
Absorption
Active Site
Activity Regulation
Binding Site BINDING 18; /note="Heme b"; /evidence="ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW"; BINDING 134; /note="Heme b"; /evidence="ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW"; BINDING 183; /note="Heme b"; /evidence="ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW"
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000269|PubMed:11121422, ECO:0000269|PubMed:7703255};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; Evidence={ECO:0000305|PubMed:7703255};
DNA Binding
EC Number 1.14.14.18
Enzyme Function FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:7703255, PubMed:11121422). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707). {ECO:0000269|PubMed:11121422, ECO:0000269|PubMed:7703255, ECO:0000303|PubMed:20055707}.; FUNCTION: [Heme oxygenase 1 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:7703255}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Binding site (3); Chain (2); Compositional bias (1); Helix (15); Metal binding (1); Modified residue (1); Mutagenesis (1); Natural variant (2); Region (1); Site (1); Topological domain (1); Transmembrane (1); Turn (1)
Keywords 3D-structure;Apoptosis;Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Oxidoreductase;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix
Interact With Q13520; Q3SXY8; P11912; O75208; Q7Z7G2; Q9BUF7-2; P49447; Q53TN4; Q9GZR5; Q9NYP7; Q9H5J4; Q9Y282; Q8TBP5; Q5JX71; Q96KR6; Q8TDT2; Q8N5M9; Q15800; Q13113; Q9NUX5; Q9BY50; O60669; Q16623; Q96MV1; Q96DZ7; Q9NUH8
Induction INDUCTION: Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. {ECO:0000269|PubMed:2911585, ECO:0000269|PubMed:3345742}.
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22419571}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000269|PubMed:22419571}.
Modified Residue MOD_RES 229; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:20068231
Post Translational Modification PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000305|PubMed:7703255}.
Signal Peptide
Structure 3D X-ray crystallography (26)
Cross Reference PDB 1N3U; 1N45; 1NI6; 1OYK; 1OYL; 1OZE; 1OZL; 1OZR; 1OZW; 1S13; 1S8C; 1T5P; 1TWN; 1TWR; 1XJZ; 1XK0; 1XK1; 1XK2; 1XK3; 3CZY; 3HOK; 3K4F; 3TGM; 4WD4; 5BTQ; 6EHA;
Mapped Pubmed ID 10631150; 10821856; 11718398; 11727267; 11786534; 11820797; 11829463; 12086318; 12091240; 12099373; 12117910; 12118938; 12130498; 12133007; 12136229; 12151344; 12153964; 12182912; 12207883; 12222997; 12356737; 12376298; 12376363; 12376366; 12377749; 12379283; 12396617; 12397597; 12433915; 12469218; 12480749; 12493432; 12500973; 12511571; 12566526; 12579334; 12585963; 12626517; 12649161; 12679469; 12690112; 12709566; 12709568; 12709569; 12709590; 12709592; 12716475; 12730098; 12736395; 12777398; 12783778; 12805077; 12810075; 12832044; 12865654; 12872043; 12891549; 12927812; 12927819; 12933701; 12941774; 12947311; 12969148; 13678532; 14521259; 14523007; 14529548; 14587309; 14615405; 14635185; 14647439; 14660632; 14683741; 14691581; 14715242; 14726403; 14733911; 14981149; 14988408; 14992466; 15004156; 15028349; 15049686; 15064108; 15084931; 15140586; 15161530; 15166181; 15184199; 15233805; 15284058; 15285018; 15297453; 15316927; 15319861; 15336443; 15337692; 15365571; 15451051; 15465821; 15470195; 15474356; 15519649; 15522396; 15525643; 15544924; 15547665; 15581622; 15611319; 15618017; 15629867; 15652505; 15661856; 15688187; 15690204; 15708368; 15741166; 15763346; 15797262; 15797755; 15805230; 15817713; 15833736; 15834587; 15849554; 15869882; 15875813; 15878918; 15885363; 15897578; 15899048; 15964514; 16020495; 16100019; 16117883; 16123320; 16154535; 16181102; 16189191; 16210136; 16232329; 16234431; 16249618; 16271489; 16309585; 16309586; 16309588; 16313248; 16319139; 16374439; 16387424; 16399210; 16455537; 16462769; 16474202; 16485041; 16495813; 16530877; 16540907; 16568091; 16582079; 16596642; 16609364; 16620829; 16697692; 16712795; 16724942; 16771696; 16772700; 16777091; 16783602; 16804400; 16840713; 16849502; 16882737; 16887359; 16923960; 16945925; 16950787; 16951197; 16971418; 16999951; 17003650; 17018862; 17020887; 17064313; 17065227; 17079780; 17095719; 17203192; 17204476; 17211576; 17216339; 17219054; 17229906; 17244614; 17254481; 17277740; 17295091; 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Motif
Gene Encoded By
Mass 32,819
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: [Heme oxygenase 1]: Kinetic parameters: KM=6 uM for heme b {ECO:0000269|PubMed:7703255}; Vmax=102 nmol/h/mg enzyme for heme b {ECO:0000269|PubMed:7703255}; ; BIOPHYSICOCHEMICAL PROPERTIES: [Heme oxygenase 1 soluble form]: Kinetic parameters: KM=3 uM for heme b {ECO:0000269|PubMed:7703255}; Vmax=40 nmol/h/mg enzyme for heme b {ECO:0000269|PubMed:7703255};
Metal Binding METAL 25; /note="Iron (heme axial ligand)"; /evidence="ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW"
Rhea ID RHEA:21764; RHEA:21765
Cross Reference Brenda 1.14.14.18;