[Novel chromophore substrates of aspartyl proteinases].
Chromophore substrates Dnp-Ala-Glu-Phe-Ala-Arg-NH2 and Dnp-Ala-Ala-Phe-Nle-Ala-Arg-NH2 of aspartic proteases were synthesized by a combination of chemical and enzymic methods. The kinetic parameters of their hydrolysis with pepsin, aspergyllopepsin, and chymosin were determined. The introduction of Nle in the P1' position gives stable enzyme-substrate complexes with pepsin and chymosin. A Glu residue at the P2 position contributes significantly to an increase in kcat for the chymosin hydrolysis.
Litvinova
O V
OV
Moscow State University, Chemical Faculty, Russia.
Balandina
G N
GN
D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002863:Chromogenic Compounds / Q000138:chemical synthesis* / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D013379:Substrate Specificity
D002863:Chromogenic Compounds; D016282:Aspartic Acid Endopeptidases
Novye khromofornye substraty aspartil'nykh proteinaz.