Structural requirements for nucleophilic substrates of carboxypeptidase Y.
نویسندگان
چکیده
منابع مشابه
Novel internally quenched fluorogenic substrates for angiotensin I-converting enzyme and carboxypeptidase Y.
Angiotensin I-converting enzyme (ACE, EC 3.4.15.1) is one of the most important enzymes in the renin-angiotensin system, a major blood pressure control system in mammals. We synthesized novel internally quenched fluorogenic (IQF) substrates for ACE based on the cleavage site of an angiotensin I, introducing N-methyl anthranic acid (Nma) and N(ε)-2,4-dinitrophenyl-lysine (Lys(Dnp))at the N- and ...
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A new carboxypeptidase (carboxypeptidase S) was found in a Saccharomyces cerevisiae strain lacking carboxypeptidase Y (D. H. Wolf and U. Weiser, Eur. J. Biochem. 73:553-556, 1977). Mutants devoid of carboxypeptidase S activity were isolated from a mutant strain that was also deficient in carboxypeptidase Y. Four mutants were analyzed in detail and fell into one complementation group. The defect...
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The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised ...
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The mechanism of action of peptide inhibitors on angiotensin I-converting enzyme (Al-converting enzyme) was studied in relation to the substrate requirements of the enzyme in vivo in the dog lung and in vitro in plasma. l-</-Asp-8-Ile-AI prepared by the solid-phase technique was compared with the known peptide inhibitors of Al-converting enzyme. BPP5il (Pyr-Lys-Trp-Ala-Pro) and SQ 20881 (Pyr-Tr...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)54783-9