calpain and benzyloxycarbonyltyrosylalanine-diazomethane

calpain has been researched along with benzyloxycarbonyltyrosylalanine-diazomethane* in 1 studies

Other Studies

1 other study(ies) available for calpain and benzyloxycarbonyltyrosylalanine-diazomethane

Article	Year
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B. The Biochemical journal, 1988, Aug-01, Volume: 253, Issue:3 A series of peptidyldiazomethanes was synthesized and tested as inactivators of the cysteine proteinases calpain II, cathepsin L and cathepsin B. Inactivators that react rapidly and that show a degree of selectivity between the enzymes were identified. Z-Tyr(I)-Ala-CHN2 (where Z represents benzyloxycarbonyl) reacts rapidly with cathepsin L and more slowly with cathepsin B, but does not inhibit calpain II. Z-Leu-Leu-Tyr-CHN2 reacts rapidly with cathepsin L and calpain II but very slowly with cathepsin B. Boc-Val-Lys(epsilon-Z)Leu-Tyr-CHN2 (where Boc represents t-butyloxycarbonyl) reacts more rapidly with calpain II than with cathepsin L or cathepsin B. The discriminating inhibitory effects of these compounds make them potentially useful for investigation of enzyme functions in vivo. The data presented also provide insights into the subsite specificity of calpain. Topics: Calpain; Cathepsin B; Cathepsin L; Cathepsins; Cysteine Endopeptidases; Diazomethane; Dipeptides; Endopeptidases; Kinetics; Oligopeptides; Protease Inhibitors; Structure-Activity Relationship	1988

Article

Year

The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B.

The Biochemical journal, 1988, Aug-01, Volume: 253, Issue:3

A series of peptidyldiazomethanes was synthesized and tested as inactivators of the cysteine proteinases calpain II, cathepsin L and cathepsin B. Inactivators that react rapidly and that show a degree of selectivity between the enzymes were identified. Z-Tyr(I)-Ala-CHN2 (where Z represents benzyloxycarbonyl) reacts rapidly with cathepsin L and more slowly with cathepsin B, but does not inhibit calpain II. Z-Leu-Leu-Tyr-CHN2 reacts rapidly with cathepsin L and calpain II but very slowly with cathepsin B. Boc-Val-Lys(epsilon-Z)Leu-Tyr-CHN2 (where Boc represents t-butyloxycarbonyl) reacts more rapidly with calpain II than with cathepsin L or cathepsin B. The discriminating inhibitory effects of these compounds make them potentially useful for investigation of enzyme functions in vivo. The data presented also provide insights into the subsite specificity of calpain.

Topics: Calpain; Cathepsin B; Cathepsin L; Cathepsins; Cysteine Endopeptidases; Diazomethane; Dipeptides; Endopeptidases; Kinetics; Oligopeptides; Protease Inhibitors; Structure-Activity Relationship

1988