| 释义 |
- References
- Further reading
- External links
{{Infobox_gene}}Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene.[1][2][3]Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues[3] References1. ^{{cite journal | vauthors = Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M | title = The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model | journal = J Biol Chem | volume = 270 | issue = 12 | pages = 6651–7 |date=Apr 1995 | pmid = 7896805 | pmc = | doi = 10.1074/jbc.270.12.6651}}
2. ^{{cite journal | vauthors = Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T | title = Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32 | journal = Genomics | volume = 66 | issue = 2 | pages = 221–5 |date=Aug 2000 | pmid = 10860668 | pmc = | doi = 10.1006/geno.2000.6206 }}
3. ^1 {{cite web | title = Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1358| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=Pascual R, Burgos FJ, Salva M |title=Purification and properties of five different forms of human procarboxypeptidases. |journal=Eur. J. Biochem. |volume=179 |issue= 3 |pages= 609–16 |year= 1989 |pmid= 2920728 |doi=10.1111/j.1432-1033.1989.tb14590.x |display-authors=etal}}
- {{cite journal | vauthors=Laethem RM, Blumenkopf TA, Cory M |title=Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. |journal=Arch. Biochem. Biophys. |volume=332 |issue= 1 |pages= 8–18 |year= 1996 |pmid= 8806703 |doi= 10.1006/abbi.1996.0310 |display-authors=etal}}
- {{cite journal | vauthors=García-Sáez I, Reverter D, Vendrell J |title=The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. |journal=EMBO J. |volume=16 |issue= 23 |pages= 6906–13 |year= 1998 |pmid= 9384570 |doi= 10.1093/emboj/16.23.6906 | pmc=1170294 |display-authors=etal}}
- {{cite journal | vauthors=Reverter D, García-Sáez I, Catasús L |title=Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2. |journal=FEBS Lett. |volume=420 |issue= 1 |pages= 7–10 |year= 1998 |pmid= 9450539 |doi=10.1016/S0014-5793(97)01476-2 |display-authors=etal}}
- {{cite journal | vauthors=Reverter D, Fernández-Catalán C, Baumgartner R |title=Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. |journal=Nat. Struct. Biol. |volume=7 |issue= 4 |pages= 322–8 |year= 2000 |pmid= 10742178 |doi= 10.1038/74092 |display-authors=etal}}
- {{cite journal | vauthors=Wouters MA, Husain A |title=Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily. |journal=J. Mol. Biol. |volume=314 |issue= 5 |pages= 1191–207 |year= 2002 |pmid= 11743734 |doi= 10.1006/jmbi.2000.5161 }}
- {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
- {{cite journal | vauthors=Jiménez MA, Villegas V, Santoro J |title=NMR solution structure of the activation domain of human procarboxypeptidase A2. |journal=Protein Sci. |volume=12 |issue= 2 |pages= 296–305 |year= 2003 |pmid= 12538893 |doi=10.1110/ps.0227303 | pmc=2312417 |display-authors=etal}}
- {{cite journal | vauthors=Dantas G, Kuhlman B, Callender D |title=A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins. |journal=J. Mol. Biol. |volume=332 |issue= 2 |pages= 449–60 |year= 2003 |pmid= 12948494 |doi=10.1016/S0022-2836(03)00888-X |display-authors=etal|citeseerx=10.1.1.66.8110 }}
- {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
- {{cite journal | vauthors=Dantas G, Corrent C, Reichow SL |title=High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design. |journal=J. Mol. Biol. |volume=366 |issue= 4 |pages= 1209–21 |year= 2007 |pmid= 17196978 |doi= 10.1016/j.jmb.2006.11.080 |pmc=3764424|display-authors=etal}}
{{refend}}External links- The MEROPS online database for peptidases and their inhibitors: M14.002
{{PDB Gallery|geneid=1358}}{{Proteases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{gene-7-stub}} 1 : EC 3.4.17 |