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 Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. FEBS J. (1742-464X) 2012 Akif M., Masuyer G., Bingham RJ., Sturrock ED., Isaac RE., Acharya KR. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Akif M., Masuyer G., Bingham RJ., Sturrock ED., Isaac RE., Acharya KR. FEBS J. (1742-464X) 2012 Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster. FEBS J. (1742-464X) 2012 Akif M., Masuyer G., Bingham RJ., Sturrock ED., Isaac RE., Acharya KR. in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Akif M., Masuyer G., Bingham RJ., Sturrock ED., Isaac RE., Acharya KR. FEBS J. (1742-464X) 2012 bnp_globl Bradykinin-potentiating and C-type natriuretic peptides Angiotensin-converting enzyme inhibitor BPP-CNP homolog protein protein mamushi Gloydius blomhoffii MFVSRLAASGLLLLALMALSLDGKPVQQWSQGRPPGPPIPRLVVQQWSQGLPPGPPIPRLVVQQWSQGLPPGPPIPPLVVQQWSQGLPPRPKIPPLVVQQWSQGLPPRPKIPPLVVQKWDPPPVSPPLLLQPHESPAGGTTALREELSLGPEAASGPAAAGADGGRSGSKAPAALHRLSKSKGASATSASASRPMRDLRTDGKQARQNWARMVNPDHHAVGGCCCGGGGGGARRLKGLVKKGVAKGCFGLKLDRIGTMSGLGC mint 407BA9A572BF5FC8 ace_drome Angiotensin-converting enzyme Ance Race CG8827 Dipeptidyl carboxypeptidase I Kininase II protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MRLFLLALLATLAVTQALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGLLKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVSS 9E3691BCC51D6C48 angt_human Angiotensinogen Serpin A8 AGT SERPINA8 protein protein human Homo sapiens Human MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA DIP protein P01019 original sequence version: 136 5026C2DFB2DD236E kng1_human Kininogen-1 KNG1 BDK KNG Alpha-2-thiol proteinase inhibitor Fitzgerald factor High molecular weight kininogen Williams-Fitzgerald-Flaujeac factor protein protein human Homo sapiens Human MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS 3132B4DF2954C24E agt-ance 1 Ang II 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain AnCE 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint t1 t2 t3 f1 f2a f3a f3b PDB code: 4AA1 ance-kng1 1 AnCE 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Bradykinin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction mint AnCE-BK peptide complex PBD code: 4ASQ AnCE-Thr6-BK peptide complex PBD code: 4ASR Unlike Ang II, BK (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) and Thr6-BK (Arg-Pro-Pro-Gly-Phe-Thr-Pro- Phe-Arg) undergo degradation by AnCE to BK1-7 and Thr6-BK 1-7, respectively and then to BK1-5 (Supplementary Fig. S2A). BK1-5 is further cleaved by AnCE to release the dipeptide Gly-Phe (Supplementary Fig. S2B) and therefore under the conditions employed in the crystallisation, it is expected that both BK and Thr6-BK will be sequentially hydrolysed to the final product, Arg-Pro- Pro. Therefore it was not surprising that the structures of AnCE in complex with BK and Thr6-BK showed Arg-Pro-Pro bound in a similar fashion in the active site cleft. (Figs. 2B,C, Tables 2,3). t1 t2 t3 f1 f2b f3c sf3 ance-bnp 1 BPP 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified AnCE 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint t1 t2 t3 f2d f3e f3f PDB code: 4AA2 ance-kng1-1 2 Bradykinin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain AnCE 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp enzyme enzyme neutral component neutral component purified purified cleavage cleavage reaction cleavage sf2 mint Unlike Ang II, BK (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) and Thr6-BK (Arg-Pro-Pro-Gly-Phe-Thr-Pro- Phe-Arg) undergo degradation by AnCE to BK1-7 and Thr6-BK 1-7, respectively and then to BK1-5 (Supplementary Fig. S2A). BK1-5 is further cleaved by AnCE to release the dipeptide Gly-Phe (Supplementary Fig. S2B) and therefore under the conditions employed in the crystallisation, it is expected that both BK and Thr6-BK will be sequentially hydrolysed to the final product, Arg-Pro- Pro. agt-ance-1 2 Ang I 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain AnCE 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp enzyme enzyme neutral component neutral component purified purified cleavage cleavage reaction cleavage sf1 mint The conversion of Ang I to Ang II (A and B) and the stability of Ang II (C and D) in the presence of recombinant AnCE.