The role of Glu196 in the environment around the substrate binding site of leucine aminopeptidase from Streptomyces griseus

FEBS Letters
Jiro ArimaTadashi Hatanaka

Abstract

To investigate the role of Glu196 of leucine aminopeptidase from Streptomyces griseus (SGAP) in SGAP activation by calcium and substrate specificity, we constructed E196X SGAP by saturation mutagenesis. Most mutations led to the abrogation of SGAP activation by calcium, and substitution with Lys led to a marked increase in activity toward Asp-p-nitroanilide (pNA) and a decrease in that toward Lys-pNA. A similar result was obtained from the investigation using non-calcium-activated enzyme from Streptomyces septatus (SSAP). These results indicate that Glu196 of SGAP is associated with the environment around the substrate binding site besides its role in SGAP activation by calcium.

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Related Concepts

Anilides
Bacterial Proteins
Calcium
Enzyme Activation
Methoxyleucine Aminopeptidase
Ligands
Streptomyces griseus
Substrate Specificity
Mutagenesis Process
Point Mutation

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