WordNet

any substance (such as an antibody) or agent that can cause lysis
an essential amino acid found in proteins; occurs especially in gelatin and casein

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リジン(細胞溶解素), = lysine

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/07/04 01:13:43」(JST)

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Lysine carboxypeptidase (EC 3.4.17.3, carboxypeptidase N, arginine carboxypeptidase, kininase I, anaphylatoxin inactivator, plasma carboxypeptidase B, creatine kinase conversion factor, bradykinase, kininase Ia, hippuryllysine hydrolase, bradykinin-decomposing enzyme, protaminase, CPase N, creatinine kinase convertase, peptidyl-L-lysine(-L-arginine) hydrolase, CPN) is an enzyme.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

Release of a C-terminal basic amino acid, preferentially lysine

This is a zinc enzyme found in plasma. It inactivates bradykinin and anaphylatoxins.

References

^ Plummer, T.H. Jr.; Erdös, E.G. (1981). "Human plasma carboxypeptidase N". Methods Enzymol. 80: 442–449. PMID 7341915. doi:10.1016/s0076-6879(81)80038-9.
^ Levin, Y.; Skidgel, R.A.; Erdös, E.G. (1982). "Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I)". Proc. Natl. Acad. Sci. USA. 79: 4618–4622. PMC 346726 . PMID 6750606. doi:10.1073/pnas.79.15.4618.
^ Skidgel, R.A. (1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 301–303. PMID 3074547. doi:10.1016/0165-6147(88)90015-6.

External links

Lysine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

Imaging analyses of coagulation-dependent initiation of fibrinolysis on activated platelets and its modification by thrombin-activatable fibrinolysis inhibitor.

Brzoska T, Suzuki Y, Sano H, Suzuki S, Tomczyk M, Tanaka H, Urano T1.
Thrombosis and haemostasis.Thromb Haemost.2017 Apr 3;117(4):682-690. doi: 10.1160/TH16-09-0722. Epub 2017 Feb 2.
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Clinical Experience with 18F-Labeled Small Molecule Inhibitors of Prostate-Specific Membrane Antigen.

Rowe SP1, Gorin MA2, Salas Fragomeni RA3, Drzezga A4, Pomper MG3.
PET clinics.PET Clin.2017 Apr;12(2):235-241. doi: 10.1016/j.cpet.2016.12.006. Epub 2017 Jan 23.
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Activated thrombin-activatable fibrinolysis inhibitor attenuates the angiogenic potential of endothelial cells: potential relevance to the breast tumour microenvironment.

Bazzi ZA1,2, Balun J1, Cavallo-Medved D3, Porter LA3, Boffa MB4.
Clinical & experimental metastasis.Clin Exp Metastasis.2017 Feb;34(2):155-169. doi: 10.1007/s10585-017-9837-y. Epub 2017 Jan 25.
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Japanese Journal

<b>Nicotianamine is a novel angiotensin-converting enzyme 2 inhibitor in soy</b><b>bean </b>

Biomedical Research 36(3), 219-224, 2015
NAID 130005083855

Novel internally quenched fluorogenic substrates for angiotensin I-converting enzyme and carboxypeptidase Y

Biomedical Research 32(6), 407-411, 2011
NAID 130004470795

トロンビン活性化線溶阻害因子による線溶活性調節機構

日本薬理学雑誌 116(5), 298-303, 2000-11-01
NAID 10008181289

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リンク元	「リジンカルボキシペプチダーゼ」
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Lysine carboxypeptidase
Identifiers
EC number	3.4.17.3
CAS number	9013-89-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
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NCBI	proteins

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英: lysine carboxypeptidase

「carboxypeptidase」

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カルボキシペプチダーゼ

[1] Plummer, T.H. Jr.; Erdös, E.G. (1981). "Human plasma carboxypeptidase N". Methods Enzymol. 80: 442–449. PMID 7341915. doi:10.1016/s0076-6879(81)80038-9.

[2] Levin, Y.; Skidgel, R.A.; Erdös, E.G. (1982). "Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I)". Proc. Natl. Acad. Sci. USA. 79: 4618–4622. PMC 346726 . PMID 6750606. doi:10.1073/pnas.79.15.4618.

[3] Skidgel, R.A. (1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 301–303. PMID 3074547. doi:10.1016/0165-6147(88)90015-6.

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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lysine carboxypeptidase