Biomaterial Database

Inhibitors of kininases. 1979

E G Erdös

UI	MeSH Term	Description	Entries
D007703	Peptidyl-Dipeptidase A	A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-\|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator; and has a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April 15, 2020).	ACE1 Angiotensin-Converting Enzyme 1,ACE1 Protein,Angiotensin Converting Enzyme,Angiotensin Converting Enzyme 1,Antigens, CD143,CD143 Antigens,Dipeptidyl Carboxypeptidase I,Kininase II,Peptidase P,Angiotensin I-Converting Enzyme,Carboxycathepsin,Dipeptidyl Peptidase A,Kininase A,ACE1 Angiotensin Converting Enzyme 1,Angiotensin I Converting Enzyme,Carboxypeptidase I, Dipeptidyl,Peptidyl Dipeptidase A
D002268	Carboxypeptidases	Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.	Carboxypeptidase
D004745	Enkephalins	One of the three major families of endogenous opioid peptides. The enkephalins are pentapeptides that are widespread in the central and peripheral nervous systems and in the adrenal medulla.	Enkephalin
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000803	Angiotensin I	A decapeptide that is cleaved from precursor angiotensinogen by RENIN. Angiotensin I has limited biological activity. It is converted to angiotensin II, a potent vasoconstrictor, after the removal of two amino acids at the C-terminal by ANGIOTENSIN CONVERTING ENZYME.
D000806	Angiotensin-Converting Enzyme Inhibitors	A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.	ACE Inhibitor,ACE Inhibitors,Angiotensin Converting Enzyme Inhibitor,Angiotensin I-Converting Enzyme Inhibitor,Angiotensin-Converting Enzyme Inhibitor,Kininase II Inhibitor,Kininase II Inhibitors,Angiotensin I-Converting Enzyme Inhibitors,Angiotensin-Converting Enzyme Antagonists,Antagonists, Angiotensin-Converting Enzyme,Antagonists, Kininase II,Inhibitors, ACE,Inhibitors, Angiotensin-Converting Enzyme,Inhibitors, Kininase II,Kininase II Antagonists,Angiotensin Converting Enzyme Antagonists,Angiotensin Converting Enzyme Inhibitors,Angiotensin I Converting Enzyme Inhibitor,Angiotensin I Converting Enzyme Inhibitors,Antagonists, Angiotensin Converting Enzyme,Enzyme Antagonists, Angiotensin-Converting,Enzyme Inhibitor, Angiotensin-Converting,Enzyme Inhibitors, Angiotensin-Converting,II Inhibitor, Kininase,Inhibitor, ACE,Inhibitor, Angiotensin-Converting Enzyme,Inhibitor, Kininase II,Inhibitors, Angiotensin Converting Enzyme
D001121	Lysine Carboxypeptidase	A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.	Carboxypeptidase N,Kininase I,Anaphylatoxin Inactivator,Bradykininase,Carboxypeptidase, Lysine,Inactivator, Anaphylatoxin
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities

Related Publications

E G Erdös

Effects of inhibitors on the in vitro inactivation of bradykinin by various kininases.

January 1965, Acta pharmacologica et toxicologica,

E G Erdös

Kininases of human polymorphonuclear leucocytes.

August 1980, Biochemical pharmacology,

E G Erdös

Studies on the kallikrein-like substances, kininases and kallikrein inhibitors in the rabbit's organs.

January 1969, Mie medical journal,

E G Erdös

Renal kininases in primary aldosteronism.

January 1989, Advances in experimental medicine and biology,

E G Erdös

Potent kininases obtained from mushrooms.

January 1976, Advances in experimental medicine and biology,

E G Erdös

[Kininases from yeasts (author's transl)].

January 1975, Zentralblatt fur Bakteriologie, Parasitenkunde, Infektionskrankheiten und Hygiene. Erste Abteilung Originale. Reihe A: Medizinische Mikrobiologie und Parasitologie,

E G Erdös

[Activity of kininases in athosclerotic patients].

February 1972, Polski tygodnik lekarski (Warsaw, Poland : 1960),

E G Erdös

Characterization of kininases in testicular cells.

May 1996, Immunopharmacology,

E G Erdös

The kininases of Bothrops jararaca plasma.

January 1980, Acta physiologica latino americana,

E G Erdös

Kininases in leucocytes and other tissues.

July 1962, Nature,