関: carboxypeptidase Y、cathepsin A

WordNet

the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system

PrepTutorEJDIC

carbonの化学記号
cesiumの化学記号
cadmiumの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/02 14:56:47」(JST)

wiki en

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. and 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. and 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. and 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)

Molecular and Cellular Biology portal

UpToDate Contents

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1. 高用量メトトレキサートの治療使用および毒性 therapeutic use and toxicity of high dose methotrexate
2. 肥満細胞由来のメディエーター mast cell derived mediators
3. アナフィラキシー：急性期診断 anaphylaxis acute diagnosis
4. アナフィラキシーの臨床診断を裏付ける臨床検査 laboratory tests to support the clinical diagnosis of anaphylaxis
5. 血栓溶解異常による血栓性および出血性疾患 thrombotic and hemorrhagic disorders due to abnormal fibrinolysis

English Journal

Activity and the metabolic activation pathway of the potent and selective hepatitis C virus pronucleotide inhibitor PSI-353661.

Furman PA, Murakami E, Niu C, Lam AM, Espiritu C, Bansal S, Bao H, Tolstykh T, Micolochick Steuer H, Keilman M, Zennou V, Bourne N, Veselenak RL, Chang W, Ross BS, Du J, Otto MJ, Sofia MJ.SourcePharmasset, Inc., Princeton, NJ 08540, USA. phillip.furman@pharmasset.com
Antiviral research.Antiviral Res.2011 Aug;91(2):120-32. Epub 2011 May 12.
PSI-353661, a phosphoramidate prodrug of 2'-deoxy-2'-fluoro-2'-C-methylguanosine-5'-monophosphate, is a highly active inhibitor of genotype 1a, 1b, and 2a HCV RNA replication in the replicon assay and of genotype 1a and 2a infectious virus replication. PSI-353661 is active against replicons harborin
PMID 21600932

Proteases in autophagy.

Kaminskyy V, Zhivotovsky B.AbstractAutophagy is a process involved in the proteolytic degradation of cellular macromolecules in lysosomes, which requires the activity of proteases, enzymes that hydrolyse peptide bonds and play a critical role in the initiation and execution of autophagy. Importantly, proteases also inhibit autophagy in certain cases. The initial steps of macroautophagy depend on the proteolytic processing of a particular protein, Atg8, by a cysteine protease, Atg4. This processing step is essential for conjugation of Atg8 with phosphatidylethanolamine and, subsequently, autophagosome formation. Lysosomal hydrolases, known as cathepsins, can be divided into several groups based on the catalytic residue in the active, namely, cysteine, serine and aspartic cathepsins, which catalyse the cleavage of peptide bonds of autophagy substrates and, together with other factors, dispose of the autophagic flux. Whilst most cathepsins degrade autophagosomal content, some, such as cathepsin L, also degrade lysosomal membrane components, GABARAP-II and LC-II. In contrast, cathepsin A, a serine protease, is involved in inhibition of chaperon-mediated autophagy through proteolytic processing of LAMP-2A. In addition, other families of calcium-dependent non-lysosomal cysteine proteases, such as calpains, and cysteine aspartate-specific proteases, such as caspases, may cleave autophagy-related proteins, negatively influencing the execution of autophagic processes. Here we discuss the current state of knowledge concerning protein degradation by autophagy and outline the role of proteases in autophagic processes. This article is part of a Special Issue entitled: Proteolysis 50years after the discovery of lysosome.
Biochimica et biophysica acta.Biochim Biophys Acta.2011 May 24. [Epub ahead of print]
Autophagy is a process involved in the proteolytic degradation of cellular macromolecules in lysosomes, which requires the activity of proteases, enzymes that hydrolyse peptide bonds and play a critical role in the initiation and execution of autophagy. Importantly, proteases also inhibit autophagy
PMID 21640203

Japanese Journal

アンジオテンシン変換酵素(ACE2)様活性をもつB38-CAPによる降圧作用と心不全改善作用

久場敬司,湊隆文,韮澤悟,佐藤輝紀,山口智和,渡邊博之,今井由美子,高橋砂織
日本薬理学会年会要旨集 93(0), 3-P-314, 2020
… Here we show that the B38-CAP, a carboxypeptidase derived from <i>Paenibacillus sp.</i> … Our data identify the bacterial B38-CAP as an ACE2-like carboxypeptidase, which exhibits ACE2-like functions in vitro and in vivo. … These results indicate that evolution has shaped a bacterial carboxypeptidase to a human ACE2-like enzyme. …
NAID 130007811864

A bacteria-derived ACE2-like enzyme suppresses cardiac remodeling and dysfunction in mice.

湊隆文,久場敬司,韮澤悟,佐藤輝紀,小澤諒,山口智和,中原和彦,渡邊博之,今井由美子,高橋砂織
日本薬理学会年会要旨集 92(0), 2-YIA-09, 2019
… We elucidate that the B38-CAP, a carboxypeptidase derived from Paenibacillus sp.B38, has ACE2-like enzymatic activity. … B38-CAP is an ACE2-like carboxypeptidase, which is functional in vitro and in vivo. …
NAID 130007813186

慢性血栓塞栓性肺高血圧症の新規病因蛋白TAFIに着目した早期診断と治療薬開発

佐藤公雄,佐藤大樹,矢尾板信裕,下川宏明
脈管学 59(8), 61-67, 2019
<p>慢性血栓塞栓性肺高血圧症（CTEPH）患者において，線溶系阻害蛋白TAFI（thrombin-activatable fibrinolysis inhibitor）の一塩基多型を発見し，血漿中の活性型TAFI上昇を認めた。さらに，TAFIの過剰発現マウスでは，CTEPH患者同様の肺動脈狭窄や途絶像，肺高血圧悪化を示し，低酸素環境3週間で40%が突然死した。創薬スクリーニングで見出 …
NAID 130007689487

「カルボキシペプチダーゼC」

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PubMed	articles
NCBI	proteins

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
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PMC	articles
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NCBI	proteins

　　[★]

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

「carboxypeptidase Y」

　　[★]

カルボキシペプチダーゼY

関: carboxypeptidase C、cathepsin A

「cathepsin A」

　　[★]

カテプシンA

関: carboxypeptidase C、carboxypeptidase Y

「C」

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「Cs」

　　[★] セシウム, caesium, cesium 　

「Cd」

　　[★] カドミウム

関: cadmium

「carboxypeptidase」

　　[★]

カルボキシペプチダーゼ

「c」

　　[★]

光速, speed of light

[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. and 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. and 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. and 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.

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

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案内

carboxypeptidase C