Carboxypeptidase B: Difference between revisions
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'''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 acts upon basic [[amino acids]], such as [[arginine]] and lysine.<ref>{{cite journal | title = Carboxypeptidase B (porcine pancreas) | | '''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 acts upon basic [[amino acids]], such as [[arginine]] and lysine.<ref>{{cite journal | title = Carboxypeptidase B (porcine pancreas) | vauthors = Folk JE |journal = Methods Enzymol. |year = 1970 |volume = 19 |pages = 504–508 |pmid = |doi=10.1016/0076-6879(70)19036-7}}</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 | 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 serum [[enzyme]] is also responsible for rapidly [[metabolizing]] the [[Complement component 5a|C5a]] [[protein]] into C5a des-Arg, with one less amino acid. | ||
== References == | == References == | ||
{{reflist}} | {{reflist}} | ||
==External links== | == External links == | ||
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M14.003 M14.003] | * The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M14.003 M14.003] | ||
* {{MeshName|Carboxypeptidase+B}} | * {{MeshName|Carboxypeptidase+B}} | ||
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{{Proteases}} | {{Proteases}} | ||
{{Enzymes}} | {{Enzymes}} | ||
{{Portal bar|Molecular and Cellular Biology|border=no}} | {{Portal bar|Molecular and Cellular Biology|Metabolism|border=no}} | ||
[[Category:EC 3.4.17]] | [[Category:EC 3.4.17]] | ||
[[Category:Metabolism]] | [[Category:Metabolism]] | ||
Revision as of 08:37, 17 February 2018
| carboxypeptidase B1 (tissue) | |
|---|---|
| Identifiers | |
| Symbol | CPB1 |
| Entrez | 1360 |
| HUGO | 2299 |
| OMIM | 114852 |
| RefSeq | NM_001871 |
| UniProt | P15086 |
| Other data | |
| EC number | 3.4.17.2 |
| Locus | Chr. 3 q24 |
| carboxypeptidase B2 (plasma) | |
|---|---|
| Identifiers | |
| Symbol | CPB2 |
| Entrez | 1361 |
| HUGO | 2300 |
| OMIM | 603101 |
| RefSeq | NM_016413 |
| UniProt | Q96IY4 |
| Other data | |
| Locus | Chr. 13 q14.11 |
| carboxypeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Carboxypeptidase B (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L-arginine]hydrolase) is a carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine.[1][2][3][4] This serum enzyme is also responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid.
References
- ↑ Folk JE (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504–508. doi:10.1016/0076-6879(70)19036-7.
- ↑ Brodrick JW, Geokas MC, Largman C (December 1976). "Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion". Biochimica et Biophysica Acta. 452 (2): 468–81. doi:10.1016/0005-2744(76)90197-2. PMID 1009123.
- ↑ Butterworth J, Duncan JJ (September 1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clinica Chimica Acta; International Journal of Clinical Chemistry. 97 (1): 39–43. doi:10.1016/0009-8981(79)90023-8. PMID 40714.
- ↑ Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD (1982). "Carboxypeptidase B activity from adrenal medulla--is it involved in the processing of proenkephalin?". Life Sciences. 31 (16–17): 1793–6. doi:10.1016/0024-3205(82)90212-0. PMID 6130442.
External links
- The MEROPS online database for peptidases and their inhibitors: M14.003
- Carboxypeptidase+B at the US National Library of Medicine Medical Subject Headings (MeSH)