MPO is a heme enzyme that uses hydrogen peroxide to oxidize chloride to hypochlorous acid. MPO reacts with hydrogen peroxide, which is produced by stimulated neutrophils, to form the redox intermediate compound I (Winterbourn CC et al 2006; Davies MJ 2011; Pattison DI et al. 2012). Compound I is strongly oxidizing and reacts with a variety of substrates such as halide and pseudo-halide ions to produce hypohalous acids (HOX where X = Cl, Br, SCN). Its main physiological substrate is assumed to be chloride, which undergoes a two-electron oxidation to form hypochlorous acid (HOCl) (Winterbourn CC et al 2006; Davies MJ 2001; Pattison DI et al. 2012).
",
"cellular_location": "phagocytic vesicle, phagocytic vesicle lumen",
"input_participant_list": [
"R-ALL-1222719",
"R-ALL-6788973"
],
"output_participant_list": [
"R-ALL-1222475",
"R-ALL-6789150"
],
"enzyme_list": [
"P05164-1"
],
"evidence": [
{
"id": "R-HSA-6789031",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6789031"
}
]
},
{
"id": "R-HSA-6789126",
"name": "Myeloperoxidase (MPO) produces hypochlorous acid (HOCl)",
"equation": "",
"summary": "Phagosomal myeloperoxidase (MPO) is an important heme enzyme released by activated leukocytes (Klebanoff SJ & Rosen H 1978; Austin GE et al. 1994; Klebanoff S 2013). MPO protein has little bactericidal effect per se, but the enzyme-generated products are chemical oxidants that have potent antibacterial, antiviral, and antifungal properties (Pattison DI et al. 2012). Ferric MPO enzyme cycles through redox intermediates that undergo a complex array of reactions. Initial oxidation of the resting iron (III) form of the enzyme by hydrogen peroxide gives rise to a primary catalytic complex, known as Compound I (Winterbourn CC et al 2006; Davies MJ 2011; Pattison DI et al. 2012). Compound I can then undergo either two electron reduction with halide or pseudo-halide ions to form hypohalous acids (HOX where X = Cl, Br, SCN) or undergo two successive one-electron reductions, via Compound II, with consequent radical formation (the peroxidase cycle) (Winterbourn CC et al 2006; Davies MJ 2011). Due to the high reduction potentials of the Compound I and II, MPO can oxidize a variety of substrates. Chloride ion is one of the physiological substrate of MPO. Cl- undergoes a two-electron oxidation to form hypochlorous acid (HOCl) (Winterbourn CC et al 2006; Davies MJ 2001; Pattison DI et al. 2012). Studies using specific probes or biomarkers such as 3-chlorotyrosine showed that MPO reacts with H2O2 and chloride present in the phagosome to produce HOCl, and that the HOCl reacts with ingested bacteria (Jiang Q et al. 1997; Palazzolo AM et al. 2005; Kenmoku S et al. 2007; Chapman AL et al. 2002; Albrett AM et al. 2018; Degrossoli A et al. 2018). Furthermore, rapid killing of numerous organisms by isolated neutrophils has been shown to require MPO (Klebanoff SJ et al. 2013; Green JN et al. 2017). HOCl reacts readily with a range of biological molecules to form potently microbicidal products such as chloramines (Green JN et al. 2017). HOCl reacts with ROS forming toxic hydroxyl radical and singlet oxygen, however the specific role of HOCl in the microbial killing remains unclear. Modelling studies indicated that phagosomal proteins could scavenge much of the HOCl before it reaches the microbe thus limiting its ability to kill (Winterbourn CC et al. 2006).",
"cellular_location": "phagocytic vesicle lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P05164-1"
],
"evidence": [
{
"id": "R-HSA-6789126",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6789126"
}
]
},
{
"id": "R-HSA-6789136",
"name": "Myeloperoxidase (MPO) binds to the bacterial cell surface",
"equation": "",
"summary": "Association of MPO with the surfaces of ingested bacteria has been observed microscopically (Selvaraj RJ et al. 1978). This could be a way of directing HOCl for effective killing (Klebanoff SJ et al. 1999). MPO has been shown to bind to the surface of a number of species (Miyasaki KT et al. 1987). However, even with MPO binding, most of the H2O2 would react with unbound MPO.",
"cellular_location": "phagocytic vesicle, plasma membrane, phagocytic vesicle lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P05164-1"
],
"evidence": [
{
"id": "R-HSA-6789136",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6789136"
}
]
},
{
"id": "R-HSA-6798751",
"name": "Exocytosis of azurophil granule lumen proteins",
"equation": "",
"summary": "Azurophil or primary granules were originally defined by their high content of myeloperoxidase (MPO) and their affinity for the basic dye azure A (Spicer & Hardin 1969). Azurophil granules are generally described as spherical. Like lysosomes, they contain CD63 in their membrane (Cham et al. 1994) but are regarded as specialized secretory granules rather than lysosomes (Cieutat et al. 1998). Azurophil granules undergo limited exocytosis in response to stimulation (Sengelov et al. 1993, Faurschou et al. 2002), their primary role is believed to be killing and degradation of engulfed microbes in the phagolysosome (Joiner et al. 1989).; ; MPO reacts with H2O2 formed by NADPH oxidase, increasing its toxicity by formation of hypochlorous acid and other chlorination products, tyrosine radicals and reactive nitrogen intermediates which attack the surface of microbes (Klebanoff et al. 2013).;",
"cellular_location": "extracellular region, azurophil granule lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05655-1",
"P07686-1",
"P12724-1",
"P04066-1",
"Q92820-1",
"Q6XQN6-1",
"Q99536-1",
"Q9BRF8-1",
"Q9UHL4-1",
"P08246-1",
"P34059-1",
"P15586-1",
"P24158-1",
"Q9Y2J8-1",
"P10619-1",
"O00584-1",
"P53396-1",
"P55072-1",
"P06280-1",
"P28482-1",
"Q9NZK5-1",
"P20933-1",
"P05089-1",
"P15289-1",
"P15848-1",
"P16278-1",
"Q9H7Z7-1",
"P53634-1",
"P08311-1",
"Q9BTY2-1",
"P00387-1",
"P30041-1",
"P05164-1",
"Q8NBS9-1",
"P11216-1",
"P10153-1",
"P61626-1",
"P08236-1",
"P42685-1",
"P07478-1",
"O00754-1",
"P20839-1"
],
"evidence": [
{
"id": "R-HSA-6798751",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6798751"
}
]
},
{
"id": "R-HSA-8933635",
"name": "Myeloperoxidase (MPO) catalyzes oxidation of nitrite to nitrogen dioxide",
"equation": "",
"summary": "Nitrite (NO2-) is the primary metabolic end product of nitric oxide (NO) that is produced by a wide variety of cell types by nitric oxide synthases (Knowles RG & Moncada S 1994). During inflammatory processes activated polymorphonuclear leukocytes are capable of converting physiological levels of nitrite (NO2-) into nitrogen dioxide (NO2) through the catalytic action of myeloperoxidase (MPO) (Van der Vliet A et al. 1997; Eiserich JP et al 1998; Burner U et al. 2000). Competition studies have demonstrated that MPO-dependent NO2- oxidation occurs in the presence of alternative anionic substrates (e.g. Cl-, Br, SCNT) suggesting that nitrite itself is a physiological substrate of mammalian peroxidase (Van der Vliet A et al. 1997). Nitrogen dioxide (NO2) can contribute to nitration of aromatic substrates such as tyrosine residue and 4-hydroxyphenyl acetic acid (HPA) during inflammatory processes (Sampson JB et al. 1998, Van der Vliet A et al. 1997; Eiserich JP et al 1998).
In the presence of hydrogen peroxide (H2O2) MPO can catalyze both one- and two-electron oxidations (Davies MJ 2011). Generally, ferric or native MPO reacts with H2O2 forming intemediate compound I (MPO-I). This redox intermediate is known to oxidize halides via a single two-electron reaction to produce the respective hypohalous acids and regenerate the native enzyme. Alternatively, stepwise reduction of compound I by two donor-derived electrons produces compound II (MPO-II) and subsequently the resting ferric state. Mechanistic studies have demonstrated that nitrite acts as an electron donor and reacts with compounds I to yield nitrogen dioxide (NO2) and compaund II. Subsequently, an additional nitrite molecule reduces compound II by one electron to regenerate a native state of MPO and to produce a second NO2 molecule (Burner U et al. 2000; Cape JC & Hurst JK 2009).", "cellular_location": "phagocytic vesicle lumen", "input_participant_list": [ "R-ALL-6789221" ], "output_participant_list": [ "R-ALL-8933637" ], "enzyme_list": [ "P05164-1" ], "evidence": [ { "id": "R-HSA-8933635", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8933635" } ] } ], "reaction_participants": [ { "participant_id": "R-ALL-1222475", "participant_name": "H2O [phagocytic vesicle lumen]", "crossref": [ { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" }, { "id": "15377", "database": "ChEBI", "url": "" }, { "id": "C00001", "database": "COMPOUND", "url": "" }, { "id": "8145132", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0002111", "database": "HMDB Metabolite", "url": "" } ] }, { "participant_id": "R-ALL-1222719", "participant_name": "H2O2 [phagocytic vesicle lumen]", "crossref": [ { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" }, { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" }, { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "HMDB0003125", "database": "HMDB Metabolite", "url": "" }, { "id": "C00027", "database": "COMPOUND", "url": "" }, { "id": "11533079", "database": "PubChem Substance", "url": "" }, { "id": "16240", "database": "ChEBI", "url": "" } ] }, { "participant_id": "R-ALL-6788973", "participant_name": "Cl- [phagocytic vesicle lumen]", "crossref": [ { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "17996", "database": "ChEBI", "url": "" }, { "id": "HMDB0000492", "database": "HMDB Metabolite", "url": "" }, { "id": "8145194", "database": "PubChem Substance", "url": "" }, { "id": "C00115", "database": "COMPOUND", "url": "" } ] }, { "participant_id": "R-ALL-6789150", "participant_name": "HOCl [phagocytic vesicle lumen]", "crossref": [ { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" }, { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" }, { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" }, { "id": "24757", "database": "ChEBI", "url": "" }, { "id": "HMDB0001050", "database": "HMDB Metabolite", "url": "" } ] }, { "participant_id": "R-ALL-6789221", "participant_name": "nitrite [phagocytic vesicle lumen]", "crossref": [ { "id": "16301", "database": "ChEBI", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "16301", "database": "ChEBI", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "16301", "database": "ChEBI", "url": "" }, { "id": "16301", "database": "ChEBI", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "16301", "database": "ChEBI", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "C00088", "database": "COMPOUND", "url": "" }, { "id": "16301", "database": "ChEBI", "url": "" } ] }, { "participant_id": "R-ALL-8933637", "participant_name": "NO2 [phagocytic vesicle lumen]", "crossref": [ { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" }, { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" }, { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" }, { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" }, { "id": "33101", "database": "ChEBI", "url": "" }, { "id": "HMDB0255649", "database": "HMDB Metabolite", "url": "" } ] } ], "reaction_enzymes": [ { "uniprot_ac": "O00584", "gene_name": "RNASET2", "activity": [ { "ec_number": "4.6.1.19", "activity": "a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+).", "evidence": [ { "id": "O00584", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00584" } ] }, { "ec_number": "4.6.1.19", "activity": "", "evidence": [ { "id": "O00584", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00584" } ] } ] }, { "uniprot_ac": "O00754", "gene_name": "MAN2B1", "activity": [ { "ec_number": "3.2.1.24", "activity": "Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.", "evidence": [ { "id": "O00754", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00754" } ] }, { "ec_number": "3.2.1.24", "activity": "", "evidence": [ { "id": "O00754", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00754" } ] } ] }, { "uniprot_ac": "P00387", "gene_name": "CYB5R3", "activity": [ { "ec_number": "1.6.2.2", "activity": "2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+).", "evidence": [ { "id": "P00387", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00387" } ] }, { "ec_number": "1.6.2.2", "activity": "", "evidence": [ { "id": "P00387", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00387" } ] } ] }, { "uniprot_ac": "P04066", "gene_name": "FUCA1", "activity": [ { "ec_number": "3.2.1.51", "activity": "an alpha-L-fucoside + H2O = an alcohol + L-fucose.", "evidence": [ { "id": "P04066", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P04066" } ] }, { "ec_number": "3.2.1.51", "activity": "", "evidence": [ { "id": "P04066", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P04066" } ] } ] }, { "uniprot_ac": "P05089", "gene_name": "ARG1", "activity": [ { "ec_number": "3.5.3.1", "activity": "H2O + L-arginine = L-ornithine + urea.", "evidence": [ { "id": "P05089", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05089" } ] }, { "ec_number": "3.5.3.1", "activity": "", "evidence": [ { "id": "P05089", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05089" } ] } ] }, { "uniprot_ac": "P05164", "gene_name": "MPO", "activity": [ { "ec_number": "1.11.2.2", "activity": "chloride + H(+) + H2O2 = H2O + hypochlorous acid.", "evidence": [ { "id": "P05164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05164" } ] }, { "ec_number": "1.11.2.2", "activity": "", "evidence": [ { "id": "P05164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05164" } ] } ] }, { "uniprot_ac": "P06280", "gene_name": "GLA", "activity": [ { "ec_number": "3.2.1.-", "activity": "", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] }, { "ec_number": "3.2.1.22", "activity": "a globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose.", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] }, { "ec_number": "3.2.1.22", "activity": "", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] } ] }, { "uniprot_ac": "P07478", "gene_name": "PRSS2", "activity": [ { "ec_number": "3.4.21.4", "activity": "Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.", "evidence": [ { "id": "P07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07478" } ] }, { "ec_number": "3.4.21.4", "activity": "", "evidence": [ { "id": "P07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07478" } ] } ] }, { "uniprot_ac": "P07686", "gene_name": "HEXB", "activity": [ { "ec_number": "3.2.1.52", "activity": "Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.", "evidence": [ { "id": "P07686", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07686" } ] }, { "ec_number": "3.2.1.52", "activity": "", "evidence": [ { "id": "P07686", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07686" } ] } ] }, { "uniprot_ac": "P08236", "gene_name": "GUSB", "activity": [ { "ec_number": "3.2.1.31", "activity": "a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate.", "evidence": [ { "id": "P08236", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08236" } ] }, { "ec_number": "3.2.1.31", "activity": "", "evidence": [ { "id": "P08236", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08236" } ] } ] }, { "uniprot_ac": "P08246", "gene_name": "ELANE", "activity": [ { "ec_number": "3.4.21.37", "activity": "Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.", "evidence": [ { "id": "P08246", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08246" } ] }, { "ec_number": "3.4.21.37", "activity": "", "evidence": [ { "id": "P08246", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08246" } ] } ] }, { "uniprot_ac": "P08311", "gene_name": "CTSG", "activity": [ { "ec_number": "3.4.21.20", "activity": "Specificity similar to chymotrypsin C.", "evidence": [ { "id": "P08311", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08311" } ] }, { "ec_number": "3.4.21.20", "activity": "", "evidence": [ { "id": "P08311", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08311" } ] } ] }, { "uniprot_ac": "P10153", "gene_name": "RNASE2", "activity": [ { "ec_number": "4.6.1.18", "activity": "an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].", "evidence": [ { "id": "P10153", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10153" } ] }, { "ec_number": "4.6.1.18", "activity": "", "evidence": [ { "id": "P10153", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10153" } ] } ] }, { "uniprot_ac": "P10619", "gene_name": "CTSA", "activity": [ { "ec_number": "3.4.16.-", "activity": "", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] }, { "ec_number": "3.4.16.5", "activity": "Release of a C-terminal amino acid with broad specificity.", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] }, { "ec_number": "3.4.16.5", "activity": "", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] } ] }, { "uniprot_ac": "P11216", "gene_name": "PYGB", "activity": [ { "ec_number": "2.4.1.1", "activity": "[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.", "evidence": [ { "id": "P11216", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11216" } ] }, { "ec_number": "2.4.1.1", "activity": "", "evidence": [ { "id": "P11216", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11216" } ] } ] }, { "uniprot_ac": "P11247", "gene_name": "Mpo", "activity": [ { "ec_number": "1.11.2.2", "activity": "chloride + H(+) + H2O2 = H2O + hypochlorous acid.", "evidence": [ { "id": "P11247", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11247" } ] }, { "ec_number": "1.11.2.2", "activity": "", "evidence": [ { "id": "P11247", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11247" } ] } ] }, { "uniprot_ac": "P12724", "gene_name": "RNASE3", "activity": [ { "ec_number": "3.1.27.-", "activity": "", "evidence": [ { "id": "P12724", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12724" } ] } ] }, { "uniprot_ac": "P15289", "gene_name": "ARSA", "activity": [ { "ec_number": "3.1.6.8", "activity": "H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate.", "evidence": [ { "id": "P15289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15289" } ] }, { "ec_number": "3.1.6.8", "activity": "", "evidence": [ { "id": "P15289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15289" } ] } ] }, { "uniprot_ac": "P15586", "gene_name": "GNS", "activity": [ { "ec_number": "3.1.6.14", "activity": "Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.", "evidence": [ { "id": "P15586", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15586" } ] }, { "ec_number": "3.1.6.14", "activity": "", "evidence": [ { "id": "P15586", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15586" } ] } ] }, { "uniprot_ac": "P15848", "gene_name": "ARSB", "activity": [ { "ec_number": "3.1.6.12", "activity": "Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.", "evidence": [ { "id": "P15848", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15848" } ] }, { "ec_number": "3.1.6.12", "activity": "", "evidence": [ { "id": "P15848", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15848" } ] } ] }, { "uniprot_ac": "P16278", "gene_name": "GLB1", "activity": [ { "ec_number": "3.2.1.23", "activity": "Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.", "evidence": [ { "id": "P16278", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16278" } ] }, { "ec_number": "3.2.1.23", "activity": "", "evidence": [ { "id": "P16278", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16278" } ] } ] }, { "uniprot_ac": "P20839", "gene_name": "IMPDH1", "activity": [ { "ec_number": "1.1.1.205", "activity": "H2O + IMP + NAD(+) = H(+) + NADH + XMP.", "evidence": [ { "id": "P20839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20839" } ] }, { "ec_number": "1.1.1.205", "activity": "", "evidence": [ { "id": "P20839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20839" } ] } ] }, { "uniprot_ac": "P20933", "gene_name": "AGA", "activity": [ { "ec_number": "3.5.1.26", "activity": "H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine.", "evidence": [ { "id": "P20933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20933" } ] }, { "ec_number": "3.5.1.26", "activity": "", "evidence": [ { "id": "P20933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20933" } ] } ] }, { "uniprot_ac": "P24158", "gene_name": "PRTN3", "activity": [ { "ec_number": "3.4.21.76", "activity": "Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.", "evidence": [ { "id": "P24158", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24158" } ] }, { "ec_number": "3.4.21.76", "activity": "", "evidence": [ { "id": "P24158", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24158" } ] } ] }, { "uniprot_ac": "P28482", "gene_name": "MAPK1", "activity": [ { "ec_number": "2.7.11.24", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P28482", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28482" } ] }, { "ec_number": "2.7.11.24", "activity": "", "evidence": [ { "id": "P28482", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28482" } ] } ] }, { "uniprot_ac": "P30041", "gene_name": "PRDX6", "activity": [ { "ec_number": "1.11.1.27", "activity": "a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O.", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "3.1.1.4", "activity": "1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "2.3.1.23", "activity": "a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA.", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "1.11.1.27", "activity": "", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] } ] }, { "uniprot_ac": "P34059", "gene_name": "GALNS", "activity": [ { "ec_number": "3.1.6.4", "activity": "Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate.", "evidence": [ { "id": "P34059", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P34059" } ] }, { "ec_number": "3.1.6.4", "activity": "", "evidence": [ { "id": "P34059", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P34059" } ] } ] }, { "uniprot_ac": "P42685", "gene_name": "FRK", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P42685", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42685" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P42685", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42685" } ] } ] }, { "uniprot_ac": "P53396", "gene_name": "ACLY", "activity": [ { "ec_number": "2.3.3.8", "activity": "acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA.", "evidence": [ { "id": "P53396", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53396" } ] }, { "ec_number": "2.3.3.8", "activity": "", "evidence": [ { "id": "P53396", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53396" } ] } ] }, { "uniprot_ac": "P53634", "gene_name": "CTSC", "activity": [ { "ec_number": "3.4.14.1", "activity": "Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.", "evidence": [ { "id": "P53634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53634" } ] }, { "ec_number": "3.4.14.1", "activity": "", "evidence": [ { "id": "P53634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53634" } ] } ] }, { "uniprot_ac": "P55072", "gene_name": "VCP", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P55072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55072" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "P55072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55072" } ] } ] }, { "uniprot_ac": "P61626", "gene_name": "LYZ", "activity": [ { "ec_number": "3.2.1.17", "activity": "Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.", "evidence": [ { "id": "P61626", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61626" } ] }, { "ec_number": "3.2.1.17", "activity": "", "evidence": [ { "id": "P61626", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61626" } ] } ] }, { "uniprot_ac": "Q05655", "gene_name": "PRKCD", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] }, { "ec_number": "2.7.11.13", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] }, { "ec_number": "2.7.11.13", "activity": "", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] } ] }, { "uniprot_ac": "Q6XQN6", "gene_name": "NAPRT", "activity": [ { "ec_number": "6.3.4.21", "activity": "5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate.", "evidence": [ { "id": "Q6XQN6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6XQN6" } ] }, { "ec_number": "6.3.4.21", "activity": "", "evidence": [ { "id": "Q6XQN6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6XQN6" } ] } ] }, { "uniprot_ac": "Q8NBS9", "gene_name": "TXNDC5", "activity": [ { "ec_number": "1.8.4.-", "activity": "", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] }, { "ec_number": "5.3.4.1", "activity": "Catalyzes the rearrangement of -S-S- bonds in proteins.", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] }, { "ec_number": "5.3.4.1", "activity": "", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] } ] }, { "uniprot_ac": "Q92820", "gene_name": "GGH", "activity": [ { "ec_number": "3.4.19.9", "activity": "(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate.", "evidence": [ { "id": "Q92820", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q92820" } ] }, { "ec_number": "3.4.19.9", "activity": "", "evidence": [ { "id": "Q92820", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q92820" } ] } ] }, { "uniprot_ac": "Q99536", "gene_name": "VAT1", "activity": [ { "ec_number": "1.-.-.-", "activity": "", "evidence": [ { "id": "Q99536", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q99536" } ] } ] }, { "uniprot_ac": "Q9BRF8", "gene_name": "CPPED1", "activity": [ { "ec_number": "3.1.3.16", "activity": "H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate.", "evidence": [ { "id": "Q9BRF8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BRF8" } ] }, { "ec_number": "3.1.3.16", "activity": "", "evidence": [ { "id": "Q9BRF8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BRF8" } ] } ] }, { "uniprot_ac": "Q9BTY2", "gene_name": "FUCA2", "activity": [ { "ec_number": "3.2.1.51", "activity": "an alpha-L-fucoside + H2O = an alcohol + L-fucose.", "evidence": [ { "id": "Q9BTY2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BTY2" } ] }, { "ec_number": "3.2.1.51", "activity": "", "evidence": [ { "id": "Q9BTY2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BTY2" } ] } ] }, { "uniprot_ac": "Q9H7Z7", "gene_name": "PTGES2", "activity": [ { "ec_number": "5.3.99.3", "activity": "prostaglandin H2 = prostaglandin E2.", "evidence": [ { "id": "Q9H7Z7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9H7Z7" } ] }, { "ec_number": "5.3.99.3", "activity": "", "evidence": [ { "id": "Q9H7Z7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9H7Z7" } ] } ] }, { "uniprot_ac": "Q9NZK5", "gene_name": "ADA2", "activity": [ { "ec_number": "3.5.4.4", "activity": "2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+).", "evidence": [ { "id": "Q9NZK5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NZK5" } ] }, { "ec_number": "3.5.4.4", "activity": "", "evidence": [ { "id": "Q9NZK5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NZK5" } ] } ] }, { "uniprot_ac": "Q9UHL4", "gene_name": "DPP7", "activity": [ { "ec_number": "3.4.14.2", "activity": "Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.", "evidence": [ { "id": "Q9UHL4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UHL4" } ] }, { "ec_number": "3.4.14.2", "activity": "", "evidence": [ { "id": "Q9UHL4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UHL4" } ] } ] }, { "uniprot_ac": "Q9Y2J8", "gene_name": "PADI2", "activity": [ { "ec_number": "3.5.3.15", "activity": "H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+).", "evidence": [ { "id": "Q9Y2J8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y2J8" } ] }, { "ec_number": "3.5.3.15", "activity": "", "evidence": [ { "id": "Q9Y2J8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y2J8" } ] } ] } ], "biomarkers": [], "synthesized_glycans": [], "cluster_types": [ { "name": "isoformset.uniprotkb", "label": "Isoforms" }, { "name": "homologset.oma", "label": "OMA Homologs" }, { "name": "homologset.mgi", "label": "MGI Homologs" } ], "sequence_features": { "n_linked_sites": [ 139, 323, 355, 391, 483, 729 ], "o_linked_sites": [ 322, 481 ], "snv_sites": [ 58, 139, 141, 154, 264, 314, 323, 325, 368, 395, 481, 483, 498, 665, 705, 729 ], "glycation_sites": [], "phosphorylation_sites": [], "sequon_annotation_sites": [ { "start_pos": 139, "end_pos": 141 }, { "start_pos": 323, "end_pos": 325 }, { "start_pos": 355, "end_pos": 357 }, { "start_pos": 391, "end_pos": 393 }, { "start_pos": 483, "end_pos": 485 }, { "start_pos": 729, "end_pos": 731 } ] }, "section_stats": [ { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 59 }, { "field": "total_sites", "count": 8 }, { "field": "n_linked_glycans", "count": 37 }, { "field": "n_linked_glycan_sites", "count": 11 }, { "field": "o_linked_glycans", "count": 2 }, { "field": "o_linked_glycan_sites", "count": 2 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", 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