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Carboxypeptidase B - Revision history
2026-05-30T19:50:55Z
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2025-01-31T11:28:58Z
<p>Added image</p>
<p><b>New page</b></p><div>{{Short description|Class of enzymes}}<br />
{{cs1 config|name-list-style=vanc}}<br />
{{protein<br />
|Name=carboxypeptidase B1 (tissue)<br />
|caption=<br />
|image=<br />
|width=<br />
|HGNCid=2299<br />
|Symbol=CPB1<br />
|AltSymbols=<br />
|EntrezGene=1360<br />
|OMIM=114852<br />
|RefSeq=NM_001871<br />
|UniProt=P15086<br />
|PDB=<br />
|ECnumber=3.4.17.2<br />
|Chromosome=3<br />
|Arm=q<br />
|Band=24<br />
|LocusSupplementaryData=<br />
}}<br />
{{protein<br />
|Name=[[carboxypeptidase B2|carboxypeptidase B2 (plasma)]]<br />
|caption=<br />
|image=<br />
|width=<br />
|HGNCid=2300<br />
|Symbol=CPB2<br />
|AltSymbols=<br />
|EntrezGene=1361<br />
|OMIM=603101<br />
|RefSeq=NM_016413<br />
|UniProt=Q96IY4<br />
|PDB=<br />
|ECnumber=<br />
|Chromosome=13<br />
|Arm=q<br />
|Band=14.11<br />
|LocusSupplementaryData=<br />
}}<br />
{{enzyme<br />
| Name = carboxypeptidase B<br />
| EC_number = 3.4.17.2<br />
| CAS_number = <br />
| IUBMB_EC_number = <br />
| GO_code = 0004180<br />
| image = <br />
| width = <br />
| caption = <br />
}}<br />
[[File:Protaminasa_-_Carboxypeptidasa_B.png | thumb | right]]<br />
'''Carboxypeptidase B''' ({{EC number|3.4.17.2}}, ''protaminase'', ''pancreatic carboxypeptidase B'', ''tissue carboxypeptidase B'', ''peptidyl-L-lysine [L-arginine]hydrolase'') is a [[carboxypeptidase]] that preferentially cleaves off basic [[amino acids]] [[arginine]] and [[lysine]] from the C-terminus of a peptide.<ref>{{cite book | title = Proteolytic Enzymes | vauthors = Folk JE | chapter = Carboxypeptidase B (Porcine Pancreas) |series = Methods Enzymol. |year = 1970 |volume = 19 |pages = 504–508 |doi=10.1016/0076-6879(70)19036-7| isbn = 9780121818814 }}</ref><ref>{{cite journal | vauthors = Brodrick JW, Geokas MC, Largman C | title = Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion | journal = Biochimica et Biophysica Acta (BBA) - Enzymology | volume = 452 | issue = 2 | pages = 468–81 | date = December 1976 | pmid = 1009123 | doi = 10.1016/0005-2744(76)90197-2 }}</ref><ref>{{cite journal | vauthors = Butterworth J, Duncan JJ | title = Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 97 | issue = 1 | pages = 39–43 | date = September 1979 | pmid = 40714 | doi = 10.1016/0009-8981(79)90023-8 }}</ref><ref>{{cite journal | vauthors = Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD | title = Carboxypeptidase B activity from adrenal medulla--is it involved in the processing of proenkephalin? | journal = Life Sciences | volume = 31 | issue = 16–17 | pages = 1793–6 | year = 1982 | pmid = 6130442 | doi = 10.1016/0024-3205(82)90212-0 }}</ref> This [[enzyme]] is secreted by the pancreas, and it travels to the small intestine, where it aids in protein digestion. Plasma carboxypeptidase B (carboxypeptidase B2) is responsible for converting the [[Complement component 5a|C5a]] [[protein]] into C5a des-Arg, with one less amino acid.<br />
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== References ==<br />
{{reflist}}<br />
<br />
== External links ==<br />
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M14.003 M14.003]<br />
* {{MeshName|Carboxypeptidase+B}}<br />
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{{Proteases}}<br />
{{Enzymes}}<br />
{{Portal|Biology}}<br />
<br />
[[Category:EC 3.4.17]]<br />
[[Category:Metabolism]]</div>
imported>Catleeball