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
|
|
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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