カルボキシペプチダーゼY
- 関
- carboxypeptidase C、cathepsin A
WordNet
- the 25th letter of the Roman alphabet (同)y, wye
PrepTutorEJDIC
- yttriumの化学記号
- y-axis
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/03/31 20:20:57」(JST)
[Wiki en表示]
| Carboxypeptidase C |
| Identifiers |
| EC number |
3.4.16.5 |
| CAS number |
9046-67-7 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Release of a C-terminal amino acid with broad specificity
This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.
See also
References
- ^ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi:10.1007/bf02907561.
- ^ Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H. (1987). "Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide". Cell. 48: 887–897. doi:10.1016/0092-8674(87)90085-7. PMID 3028649.
- ^ Jackman, H.L.; Morris, P.W.; Deddish, P.A.; Skidgel, R.A.; Erdös, E.G. (1992). "Inactivation of endothelin I by deamidase (lysosomal protective protein)". J. Biol. Chem. 267: 2872–2875. PMID 1737744.
- ^ Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. Chromatogr. 627: 153–162. doi:10.1016/0021-9673(92)87195-e. PMID 1487525.
External links
- Carboxypeptidase C 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 |
|
|
Enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
|
UpToDate Contents
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English Journal
- Luminal Ca2+ depletion during the unfolded protein response in Xenopus oocytes: cause and consequence.
- Paredes RM, Bollo M, Holstein D, Lechleiter JD.SourceDepartment of Cellular and Structural Biology, University of Texas Health Science Center at San Antonio (UTHSCSA), San Antonio, TX 78229-3900, USA.
- Cell calcium.Cell Calcium.2013 Apr;53(4):286-96. doi: 10.1016/j.ceca.2013.01.002. Epub 2013 Feb 12.
- The endoplasmic reticulum (ER) is a Ca(2+) storing organelle that plays a critical role in the synthesis, folding and post-translational modifications of many proteins. The ER enters into a condition of stress when the load of newly synthesized proteins exceeds its folding and processing capacity. T
- PMID 23415071
- Synthesis and biological evaluation of purine 2'-fluoro-2'-deoxyriboside ProTides as anti-influenza virus agents.
- Meneghesso S, Vanderlinden E, Brancale A, Balzarini J, Naesens L, McGuigan C.SourceSchool of Pharmacy and Pharmaceutical Sciences, Cardiff University, Cardiff CF10 3NB, UK. meneghessos@cardiff.ac.uk
- ChemMedChem.ChemMedChem.2013 Mar;8(3):415-25. doi: 10.1002/cmdc.201200562. Epub 2013 Feb 5.
- 2'-Fluoro-2'-deoxyguanosine has been reported to have potent anti-influenza virus activity in vitro and in vivo. Herein we describe the synthesis and biological evaluation of 6-modified 2'-fluoro-2'-deoxyguanosine analogues and their corresponding phosphoramidate ProTides as potential anti-influenza
- PMID 23386468
Japanese Journal
- Schizosaccharomyces pombe Pep12p is required for vacuolar protein transport and vacuolar homotypic fusion(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)
- Hosomi Akira,Nakase Mai,Takegawa Kaoru
- Journal of bioscience and bioengineering 112(4), 309-314, 2011-10
- … Deletion of the fission yeast pep12^+ gene results in pleiotropic phenotypes consistent with the absence of normal vacuoles, including missorting of vacuolar carboxypeptidase Y-and various ion- and drug-sensitivities. …
- NAID 110008761483
- Enzymatic Properties of the Recombinant Serine-Type Carboxypeptidase OcpC, Which Is Unique to Aspergillus oryzae
- MORITA Hiroto,ABO Haruka,OKAMOTO Ayako,MAEDA Hiroshi,YAMAGATA Youhei,KUSUMOTO Ken-Ichi,AMANO Hitoshi,ISHIDA Hiroki,TAKEUCHI Michio
- Bioscience, biotechnology, and biochemistry 75(4), 662-668, 2011-04-23
- … flavus NRRL3357, and is speculated to encode a serine-type carboxypeptidase. … Purified recombinant OcpC exhibited the enzymatic properties of a serine-type carboxypeptidase. …
- NAID 10028271319
Related Links
- I.U.B.: 3.4.16.5 C.A.S.: 9046-67-7. Enzymatic Reaction (image will open in a new window). Carboxypeptidase Y (CPDY) is a glycoprotein exopeptidase of the acid and serine class. History: CPDY was originally referred to as proteinase C by ...
- Source: Yeast I.U.B.: 3.4.16.5. Carboxypeptidase Y is a glycoprotein exopeptidase of the 'acid' and 'serine' class. Carboxypeptidase Y has a broad amino acid specificity, including proline and amidated amino acid residues. Unit Definition: ...
★リンクテーブル★
[★]
- 英
- carboxypeptidase Y
- 関
- カテプシンA、カルボキシペプチダーゼC
[★]
カルボキシペプチダーゼC
- 関
- carboxypeptidase Y、cathepsin A
[★]
カテプシンA
- 関
- carboxypeptidase C、carboxypeptidase Y
[★]
[★]
カルボキシペプチダーゼ