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 http://mint.bio.uniroma2.it/mint chew-2005-1 Ubiquitin and ubiquitin-derived peptides as substrates for peptidylglycine alpha-amidating monooxygenase. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Chew GH., Galloway LC., McIntyre NR., Schroder LA., Richards KM., Miller SA., Wright DW., Merkler DJ. 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 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 fau-pam 210503 ubim_bovin 210504 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified Stoichiometry: 1.0 amd_bovin 210505 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence enzyme enzyme unspecified role unspecified role purified purified Stoichiometry: 1.0 amidation amidation reaction amidation false false false F3 mint