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Titolo:
Studies on the subsite specificity of rat nardilysin (N-arginine dibasic convertase)
Autore:
Chow, KM; Csuhai, E; Juliano, MA; St Pyrek, J; Juliano, L; Hersh, LB;
Indirizzi:
Univ Kentucky, Dept Biochem, Lexington, KY 40563 USA Univ Kentucky Lexington KY USA 40563 ept Biochem, Lexington, KY 40563 USA Univ Kentucky, Mass Spectrometry Facil, Lexington, KY 40563 USA Univ Kentucky Lexington KY USA 40563 metry Facil, Lexington, KY 40563 USA Escola Paulista Med, Dept Biophys, BR-04034 Sao Paulo, Brazil Escola Paulista Med Sao Paulo Brazil BR-04034 BR-04034 Sao Paulo, Brazil Transylvania Univ, Dept Chem, Lexington, KY 40508 USA Transylvania Univ Lexington KY USA 40508 pt Chem, Lexington, KY 40508 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 26, volume: 275, anno: 2000,
pagine: 19545 - 19551
SICI:
0021-9258(20000630)275:26<19545:SOTSSO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
INSULIN-DEGRADING ENZYME; PROTEASE-III; RESIDUES; CLONING; BINDING; TISSUE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Hersh, LB Univ Kentucky, Dept Biochem, 800 Rose St, Lexington, KY 40563 USA Univ Kentucky 800 Rose St Lexington KY USA 40563 n, KY 40563 USA
Citazione:
K.M. Chow et al., "Studies on the subsite specificity of rat nardilysin (N-arginine dibasic convertase)", J BIOL CHEM, 275(26), 2000, pp. 19545-19551

Abstract

The subsite specificity of rat nardilysin was investigated using fluorogenic substrates of the type 2-amino-benzoyl-GGX(1)X(2)RKX(3)GQ-ethylenediamine-2,4-dinitrophenyl, where P-2, P-2', and P-3 residues were varied. (The nomenclature of Schechter and Berger (Schechter, L, and Berger, A. (1967) Biochem, Biophys, Res. Commun, 27, 157-162) is used where cleavage of a peptide occurs between the P-1 and P-1' residues, and adjacent residues are designated P-2, P-3, P-2', P-3', etc. ) There was little effect on II, among different residues at any of these positions, In contrast, residues at each position affected k(cat), with P-2 residues having the greatest effect, The S-3, S-2, and S-2' subsites differed in their amino acid preference, Tryptophan and serine, which produced poor substrates at the P-2 position, were among the best P-2' residues, The specificity at P-3 was generally opposite that of P-2. Residues at P-2, and to a lesser extent at P-3, influenced the cleavage site. At the P-2 position, His, Phe, Tyr,Asn, or Trp produced cleavage at the amino side of the first basic residue. In contrast, a P-2 Ile orVal produced cleavage between the dibasic pair, Other residues produced intermediate effects, The pH dependence for substrate binding showed that theenzyme prefers to bind a protonated histidine, A comparison of the effect of arginine or lysine at the P-1' or P-1 position showed that there is a tendency to cleave on the amino side of arginine and that this cleavage produces the highest k(cat) values.

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Documento generato il 05/12/20 alle ore 01:15:09