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Carboxypeptidase B

From Wikipedia, the free encyclopedia
Class of enzymes

carboxypeptidase B1 (tissue)
Identifiers
SymbolCPB1
NCBI gene1360
HGNC2299
OMIM114852
RefSeqNM_001871
UniProtP15086
Other data
EC number3.4.17.2
LocusChr. 3q24
Search for
StructuresSwiss-model
DomainsInterPro
carboxypeptidase B2 (plasma)
Identifiers
SymbolCPB2
NCBI gene1361
HGNC2300
OMIM603101
RefSeqNM_016413
UniProtQ96IY4
Other data
LocusChr. 13q14.11
Search for
StructuresSwiss-model
DomainsInterPro
carboxypeptidase B
Identifiers
EC no.3.4.17.2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDBPDBePDBsum
Gene OntologyAmiGO /QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Carboxypeptidase B (EC3.4.17.2,protaminase,pancreatic carboxypeptidase B,tissue carboxypeptidase B,peptidyl-L-lysine [L-arginine]hydrolase) is acarboxypeptidase that preferentially cleaves off basicamino acidsarginine andlysine from the C-terminus of a peptide.[1][2][3][4] Thisenzyme 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 theC5aprotein into C5a des-Arg, with one less amino acid.

References

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  1. ^Folk JE (1970). "Carboxypeptidase B (Porcine Pancreas)".Proteolytic Enzymes. Methods Enzymol. Vol. 19. pp. 504–508.doi:10.1016/0076-6879(70)19036-7.ISBN 9780121818814.
  2. ^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 (BBA) - Enzymology.452 (2):468–81.doi:10.1016/0005-2744(76)90197-2.PMID 1009123.
  3. ^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.
  4. ^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

[edit]
3.4.11-19:Exopeptidase
3.4.11
3.4.13
3.4.14
3.4.15
3.4.16
3.4.17
Other/ungrouped
3.4.21-25:Endopeptidase
3.4.99: Unknown
Activity
Regulation
Classification
Kinetics
Types
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