カルボキシペプチダーゼB
WordNet
- the 2nd letter of the Roman alphabet (同)b
 
- the blood group whose red cells carry the B antigen (同)type_B, group B
 
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/02/04 20:42:49」(JST)
[Wiki en表示]
| 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 / EGO | 
| Search | 
 
| PMC | 
articles | 
 
| PubMed | 
articles | 
 
| NCBI | 
proteins | 
 
 
 | 
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, J.E. (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504–508. doi:10.1016/0076-6879(70)19036-7. 
 
- ^ Brodrick, J.W., Geokas, M.C. and Largman, C. (1976). "Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion". Biochim. Biophys. Acta 452: 468–481. doi:10.1016/0005-2744(76)90197-2. PMID 1009123. 
 
- ^ Butterworth, J. and Duncan, J.J. (1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clin. Chim. Acta 97: 39–43. doi:10.1016/0009-8981(79)90023-8. PMID 40714. 
 
- ^ Wallace, E.F., Evans, C.J., Jurik, S.M., Mefford, I.N. and Barchas, J.D. (1982). "Carboxypeptidase B activity from adrenal medulla. Is it involved in the processing of proenkephalin?". Life Sci. 31: 1793–1796. 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)
 
| 
 Hydrolase: proteases (EC 3.4) 
 | 
 
 | 
 
| 3.4.11-19: Exopeptidase | 
| 3.4.11 | 
- Aminopeptidase
- Alanine
 
- Arginyl
 
- Aspartyl
 
- Cystinyl
 
- Leucyl
 
- Glutamyl
 
- Methionyl
 
- O
 
 
 
 
 
 | 
 
 | 
 
| 3.4.13 | 
 | 
 
 | 
 
| 3.4.14 | 
- Dipeptidyl peptidase
- Cathepsin C
 
- Dipeptidyl peptidase-4
 
 
 
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
 
- Tripeptidyl peptidase II
 
 
 
 
 
 | 
 
 | 
 
| 3.4.15 | 
- Angiotensin-converting enzyme
 
 
 
 | 
 
 | 
 
| 3.4.16 | 
- Serine type carboxypeptidases: Cathepsin A
 
- DD-transpeptidase
 
 
 
 | 
 
 | 
 
| 3.4.17 | 
- Metalloexopeptidases
 
- Carboxypeptidase
- A
 
- A2
 
- B
 
- C
 
- E
 
- Glutamate II
 
 
 
 
 
 | 
 
 | 
 
| Other/ungrouped | 
 | 
 
 
 | 
 
 | 
 
| 3.4.21-25: Endopeptidase | 
- Serine protease
 
- Cysteine protease
 
- Aspartic acid protease
 
- Metalloendopeptidase
 
- Threonine endopeptidase
- Proteasome endopeptidase complex
 
- HslU—HslV peptidase
 
 
 
 
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
 
- Beta-secretase 1
 
- Beta-secretase 2
 
- Gamma secretase
 
 
 
 
 
 | 
 
 | 
 
| 3.4.99: Unknown | 
 | 
 
 | 
 
- Biochemistry overview
 
- Enzymes overview
 
- By EC number: 1.1
- 2
 
- 3
 
- 4
 
- 5
 
- 6
 
- 7
 
- 8
 
- 9
 
- 10
 
- 11
 
- 12
 
- 13
 
- 14
 
- 15-99
 
 
 
- 2.1
 
- 3.1
 
- 4.1
 
- 5.1
 
- 6.1-3
 
 
 
 | 
 
 
 | 
 
 
 
 | 
 
 
 | 
| 
 Proteins: enzymes 
 | 
 
 | 
 
| Activity | 
- Active site
 
- Binding site
 
- Catalytic triad
 
- Oxyanion hole
 
- Enzyme promiscuity
 
- Catalytically perfect enzyme
 
- Coenzyme
 
- Cofactor
 
- Enzyme catalysis
 
- Enzyme kinetics
 
- Lineweaver–Burk plot
 
- Michaelis–Menten kinetics
 
 
 
 | 
 
 | 
 
| Regulation | 
- Allosteric regulation
 
- Cooperativity
 
- Enzyme inhibitor
 
 
 
 | 
 
 | 
 
| Classification | 
- EC number
 
- Enzyme superfamily
 
- Enzyme family
 
- List of enzymes
 
 
 
 | 
 
 | 
 
| Types | 
- EC1 Oxidoreductases(list)
 
- EC2 Transferases(list)
 
- EC3 Hydrolases(list)
 
- EC4 Lyases(list)
 
- EC5 Isomerases(list)
 
- EC6 Ligases(list)
 
 
 
 | 
 
 | 
 
- Biochemistry overview
 
- Enzymes overview
 
- By EC number: 1.1
- 2
 
- 3
 
- 4
 
- 5
 
- 6
 
- 7
 
- 8
 
- 9
 
- 10
 
- 11
 
- 12
 
- 13
 
- 14
 
- 15-99
 
 
 
- 2.1
 
- 3.1
 
- 4.1
 
- 5.1
 
- 6.1-3
 
 
 
 | 
 
 
 | 
 
 
 
 | 
 
 
 | 
 
UpToDate Contents
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English Journal
- Cathepsin L of Triatoma brasiliensis (Reduviidae, Triatominae): Sequence characterization, expression pattern and zymography.
 
- Waniek PJ, Pacheco Costa JE, Jansen AM, Costa J, Araújo CA.SourceLaboratório de Biologia de Tripanosomatídeos, FIOCRUZ, Avenida Brasil, 4365 Manguinhos, Rio de Janeiro, Brazil.
 
- Journal of insect physiology.J Insect Physiol.2012 Jan;58(1):178-87. Epub  2011 Nov 13.
 
- Triatoma brasiliensis is considered one of the main vectors of Chagas disease commonly found in semi-arid areas of northeastern Brazil. These insects use proteases, such as carboxypeptidase B, aminopeptidases and different cathepsins for blood digestion. In the present study, two genes encoding cath
 
- PMID 22100382
 
- Comparison of two-dimensional gel electrophoresis patterns and MALDI-TOF MS analysis of therapeutic recombinant monoclonal antibodies trastuzumab and rituximab.
 
- Nebija D, Kopelent-Frank H, Urban E, Noe CR, Lachmann B.SourceDepartment of Medicinal Chemistry, Faculty of Life Sciences, University of Vienna, Vienna, Austria.
 
- Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2011 Dec 5;56(4):684-91. Epub  2011 Jul 18.
 
- The principal objective of this study was the evaluation of two-dimensional gel electrophoresis (2-DE) in combination with MALDI-TOF MS, after tryptic digest with regard to suitability for qualitative characterization and identification of therapeutic recombinant monoclonal antibodies trastuzumab an
 
- PMID 21813259
 
Japanese Journal
- An Investigation into the Gastrointestinal Stability of Exenatide in the Presence of Pure Enzymes, Everted Intestinal Rings and Intestinal Homogenates
 
- 2P-131 清酒麹菌Aspergillus oryzae のACPase 遺伝子破壊株の酒質特性(醸造学,醸造工学,一般講演)
 
- ISP-2-2 Immunohistochemical study of serpin peptidase inhibitor B2 and carboxypeptidase A4 in uterine cervical lesions(Group 2 Oncology 2,IS Poster,International Session)
 
Related Links
- I.U.B.: 3.4.17.2 C.A.S.: 9025-24-5 Enzymatic Reaction (image will open in a new window) Carboxypeptidase B (CPDB) is a metallocarboxypeptidase that catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ...
 
- carboxypeptidase B (1) The term recommended by the IUBMB for the enzyme EC 3.4.17.2, which catalyses preferential release of C-terminal lysine or arginine. (2) Lysine carboxypeptidase, EC 3.4.17.3. car·box·y·pep·ti·dase B (kar ...
 
★リンクテーブル★
  [★]
- Mg2+存在下でC3, B, Dが反応してC3bBbとなり、これがC3転換酵素(C3bBb)あるいはC5転換酵素(C3bBb3b)を形成する。これらはP(properdin)と結合して活性化し、それぞれC3、C5を活性化する
 
 
 
  [★]
カルボキシペプチダーゼ