MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Ubiquitin and ubiquitin-derived peptides as substrates for peptidylglycine alpha-amidating monooxygenase. Ubiquitin and ubiquitin-derived peptides as substrates for peptidylglycine alpha-amidating monooxygenase. FEBS Lett. (0014-5793) 2005 imex curation Chew GH., Galloway LC., McIntyre NR., Schroder LA., Richards KM., Miller SA., Wright DW., Merkler DJ. no 2009-01-08 Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Chew GH., Galloway LC., McIntyre NR., Schroder LA., Richards KM., Miller SA., Wright DW., Merkler DJ. no FEBS Lett. (0014-5793) 2005 2009-01-08 Only protein-protein interactions imex curation ubim_bovin Ubiquitin-like protein FUBI FAU protein protein bovin Bos taurus (Bovine) Bovine MQLFVRAQELHTLEVTGQETVAQIKAHVASLEGIAPEDQVLLLAGTPLEDEATLGQCGVEALSTLEVAGRMLGG mint 379438DCAA7B9C87 amd_bovin Peptidyl-glycine alpha-amidating monooxygenase PAM protein protein bovin Bos taurus (Bovine) Bovine MAGFRSLLVLLLVFPSGCVGFRSPLSVFKRFKETTRSFSNECLGTTRPVIPIDSSDFALDIRMPGVTPKQSDTYFCMSVRLPMDEEAFVIDFKPRASMDTVHHMLLFGCNMPASTGNYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPPGGKVVNSDISCHYKKYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFTGEGRTEVTHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDIFRTIPPEANIPIPVKSDMVMMHGHHKETENKDKTSLLQQPKREEEGVLEQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDTRESAEQERGNAILVRDRIHKFHRLVSTLRPAESRVLSLQQPLPGEGTWEPEHTGDFHVEEALDWPGVYLLPGQVSGVALDPQNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPKSKEGPLLTLGRSMQPGSDQNHFCQPTDVAVDPDTGTIYVSDGYCNSRLVQFSPSGKFITQWGEASLESSPKPGQFRVPHSLALVPPLGQLCVADRENGRIQCFKTDTKEFVREIKHPSFGRNVFAISYIPGLLFAVNGKPYFEDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIAASEDGTVYVGDAHTNTVWKFTSTEKMEHRSVKKAGIEVQEIKESEAVVETKMENKPASSELQKIQEKQKLVKEPGSGVPAVLITTLLVIPVVVLLAIALFIRWKKSRAFGDSERKLEASSGRVLGRLRGKGGGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKDEDASESEEEYSAPPPAPAPSS mint Bifunctional enzyme that catalyzes 2 sequencial steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity EBD41F83E341BAF1 fau-pam 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme enzyme unspecified role unspecified role purified purified Stoichiometry: 1.0 amidation amidation reaction amidation F3 FEBS-Letters mint