関: carboxypeptidase C、cathepsin A

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the 25th letter of the Roman alphabet (同)y, wye

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yttriumの化学記号
y-axis

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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)

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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.

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)

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

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リンク元	「カルボキシペプチダーゼY」「carboxypeptidase C」「cathepsin A」
関連記事	「Y」「carboxypeptidase」

「カルボキシペプチダーゼY」

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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
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　　[★]

英: carboxypeptidase Y
関: カテプシンA、カルボキシペプチダーゼC

「carboxypeptidase C」

　　[★]

カルボキシペプチダーゼC

関: carboxypeptidase Y、cathepsin A

「cathepsin A」

　　[★]

カテプシンA

関: carboxypeptidase C、carboxypeptidase Y

「Y」

　　[★]

「carboxypeptidase」

　　[★]

カルボキシペプチダーゼ

[1] Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi:10.1007/bf02907561.

[2] 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.

[3] 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.

[4] 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.

v t e 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)

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案内

carboxypeptidase Y