Allosteric activation of chymotrypsin-catalyzed hydrolysis of specific substrates
1973; Elsevier BV; Volume: 52; Issue: 1 Linguagem: Inglês
10.1016/0006-291x(73)90975-3
ISSN1090-2104
AutoresBernard F. Erlanger, N. H. Wassermann, A. G. Cooper,
Tópico(s)Nitric Oxide and Endothelin Effects
ResumoThe rates of hydrolysis of three specific substrates of chymotrypsin, glutaryl-L-phenylalanine p-nitroanilide, acetyl-DL-tyrosine p-nitroanilide and acetyl-L-tyrosine anilide were enhanced by 2,2′-bis[α-(benzyldimethylammonium)methyl] azobenzene dibromide and less so by related compounds. Detailed studies with glutaryl-L-phenylalanine p-nitroanilide showed a 42-fold increase in kcat with no change in Km. No acceleration (or inhibition) was noted with esters, hydroxamides or proteins as substrates. Tryptic hydrolysis of benzoyl-DL-arginine p-nitroanilide was unaffected. It was concluded that certain quaternary compounds can act as allosteric effectors of chymotrypsin.
Referência(s)