N-anthraniloyl-Ala-Ala-Phe-4-nitroanilide, a highly sensitive substrate for subtilisins.

doi:10.1016/0003-9861(92)90744-H

Paper

N-anthraniloyl-Ala-Ala-Phe-4-nitroanilide, a highly sensitive substrate for subtilisins.

Published May 1, 1992 · N. Stambolieva, I. Ivanov, V. Yomtova

Archives of biochemistry and biophysics

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Abstract

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In Vitro Study

Study Snapshot

The new substrate, anthraniloyl-Ala-Ala-Phe-4-nitroanilide, offers extremely sensitive detection of subtilisins, with specificity constants 10-fold higher than those of the widely used succinyl-Ala-Ala-Pro Phe-4-nitroanil

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

N-anthraniloyl-Ala-Ala-Phe-4-nitroanilide, a highly sensitive substrate for subtilisins.

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References

Citations

Synthesis and inhibition properties of a series of pyranose derivatives towards a Zn-metalloproteinase from Saccharomonospora canescens.

A series of arabinopyranosides and glucopyranosides show potential as competitive inhibitors of the Zn-metalloproteinase from Saccharomonospora canescens, with structures that fit the S1-subsite and protect the active site Zn2+.

Expression of recombinant Plasmodium falciparum subtilisin-like protease-1 in insect cells. Characterization, comparison with the parasite protease, and homology modeling.

Recombinant PfSUB-1 shows high calcium requirements, alkaline pH optimum, relaxed substrate specificity, and similar properties to the parasite-derived enzyme, suggesting potential roles in host cell invasion and post-invasion events.

Arylamidase activity of neutral proteinase from Saccharomonospora canescens. Comparison with other Zn-proteinases that exhibit the same activity.

The arylamidase activity of Zn-proteinase from Saccharomonospora canescens is correlated with specific active site characteristics, such as penta-coordinated Zn2+ and a tyrosyl residue as a fifth ligand.

Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS).

Intramolecular fluorescence energy transfer substrates (IFETS) offer high sensitivity and selectivity in assaying proteinases, making them a promising tool for enzymology and medicine.

Expression of LA45 reactive beta 2-microglobulin free HLA class I alpha-chains on activated T-cells is regulated by internalization, constitutive and protein kinase C inducible release.

The expression of free HLA alpha-chains on activated T cells is regulated by two distinct mechanisms: constitutive release and protein kinase C inducible release.