Carboxypeptidase A2

Carboxypeptidase A2

Carboxypeptidase A2 (pancreatic), also known as CPA2, is a human gene.cite web | title = Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)| url =| accessdate = ]

section_title =
summary_text = 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 residuescite web | title = Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)| url =| accessdate = ]


Further reading

citations =
*cite journal | author=Pascual R, Burgos FJ, Salva M, "et al." |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=
*cite journal | author=Catasús L, Vendrell J, Avilés FX, "et al." |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 |year= 1995 |pmid= 7896805 |doi=
*cite journal | author=Laethem RM, Blumenkopf TA, Cory M, "et al." |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
*cite journal | author=García-Sáez I, Reverter D, Vendrell J, "et al." |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
*cite journal | author=Reverter D, García-Sáez I, Catasús L, "et al." |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=
*cite journal | author=Reverter D, Fernández-Catalán C, Baumgartner R, "et al." |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
*cite journal | author=Hayashida S, Yamasaki K, Asada Y, "et al." |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 |year= 2000 |pmid= 10860668 |doi= 10.1006/geno.2000.6206
*cite journal | author=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 | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Jiménez MA, Villegas V, Santoro J, "et al." |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=
*cite journal | author=Dantas G, Kuhlman B, Callender D, "et al." |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=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Dantas G, Corrent C, Reichow SL, "et al." |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

update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes

Wikimedia Foundation. 2010.

Игры ⚽ Поможем сделать НИР

Look at other dictionaries:

  • Carboxypeptidase E — Carboxypeptidase E, also known as CPE, is a human gene.cite web | title = Entrez Gene: CPE carboxypeptidase E| url = Cmd=ShowDetailView TermToSearch=1363| accessdate = ] PBB Summary section title …   Wikipedia

  • Carboxypeptidase — (EC number 3.4.16 3.4.18) is an enzyme that hydrolyzes the carboxy terminal (C terminal) end of a peptide bond. Humans, animals, and plants contain several types of carboxypeptidases with diverse functions ranging from catabolism to protein… …   Wikipedia

  • Carboxypeptidase B2 — (plasma) Rendering based on PDB 3D66 …   Wikipedia

  • Carboxypeptidase A — usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C terminal residues with aromatic or aliphatic side chains. Most scientists in the field now refer to this enzyme as Gene|CPA1, and to a related pancreatic… …   Wikipedia

  • Carboxypeptidase — Carboxypeptidasen Enzymklassifikation EC, Kategorie …   Deutsch Wikipedia

  • Carboxypeptidase B — protein Name=carboxypeptidase B1 (tissue) caption= width= HGNCid=2299 Symbol=CPB1 AltSymbols= EntrezGene=1360 OMIM=114852 RefSeq=NM 001871 UniProt=P15086 PDB= ECnumber= Chromosome=3 Arm=q Band=24 LocusSupplementaryData=protein… …   Wikipedia

  • carboxypeptidase — Enzymes (particularly of pancreas) that remove the C terminal amino acid from a protein or peptide. Carboxypeptidase A, (EC will remove any amino acid; carboxypeptidase B (EC is specific for terminal lysine or arginine …   Dictionary of molecular biology

  • carboxypeptidase C — See serine carboxypeptidase …   Medical dictionary

  • carboxypeptidase — karboksipeptidazė statusas T sritis chemija apibrėžtis Fermentas, atskeliantis C galines aminorūgštis. atitikmenys: angl. carboxypeptidase rus. карбоксипептидаза …   Chemijos terminų aiškinamasis žodynas

  • carboxypeptidase — noun Date: 1935 an enzyme that hydrolyzes peptides and especially polypeptides by splitting off sequentially the amino acids at the end of the peptide chain which contain free carboxyl groups …   New Collegiate Dictionary

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”