A peptidyl-glycine alpha-amidating monooxygenase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P19021]
PAM
Timeframe | Studies on this Protein(%) | All Drugs % |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
aceturic acid | Homo sapiens (human) | Km | 8,700.0000 | 2 | 2 |
prolylglycine | Homo sapiens (human) | Km | 930.0000 | 2 | 2 |
phenylalanylglycine | Homo sapiens (human) | Km | 6,250.0000 | 2 | 2 |
This protein enables 7 target(s):
Target | Category | Definition |
---|---|---|
peptidylglycine monooxygenase activity | molecular function | Catalysis of the reaction: peptidyl-glycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O. [EC:1.14.17.3] |
peptidylamidoglycolate lyase activity | molecular function | Catalysis of the reaction: peptidylamidoglycolate = peptidyl amide + glyoxylate. [EC:4.3.2.5] |
copper ion binding | molecular function | Binding to a copper (Cu) ion. [GOC:ai] |
calcium ion binding | molecular function | Binding to a calcium ion (Ca2+). [GOC:ai] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
L-ascorbic acid binding | molecular function | Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. [GOC:mah] |
This protein is located in 4 target(s):
Target | Category | Definition |
---|---|---|
membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
transport vesicle membrane | cellular component | The lipid bilayer surrounding a transport vesicle. [GOC:mah] |
secretory granule membrane | cellular component | The lipid bilayer surrounding a secretory granule. [GOC:mah] |
extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
This protein is active in 1 target(s):
Target | Category | Definition |
---|---|---|
extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
This protein is involved in 3 target(s):
Target | Category | Definition |
---|---|---|
peptide amidation | biological process | The posttranslational conversion of C-terminal glycine-extended peptides to C-terminal alpha-amidated peptides. Occurs to over half of all peptide hormones to give bioactive peptides. This is a two step process catalyzed by a peptidyl-glycine alpha-hydroxylating monooxygenase and a peptidyl-alpha-hydroxyglycine alpha-amidating lyase. In some organisms, this process is catalyzed by two separate enzymes, whereas in higher organisms, one polypeptide catalyzes both reactions. [PMID:11028916] |
response to zinc ion | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a zinc ion stimulus. [GOC:sm] |
fatty acid primary amide biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of a fatty acid primary amide. [PMID:10079066, PMID:15952893] |