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

Arima Jiro | Zendy; Uesugi Yoshiko | Zendy; Uraji Misugi | Zendy; Iwabuchi Masaki | Zendy; Hatanaka Tadashi | Zendy

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

Author(s) -

Arima Jiro,

Uesugi Yoshiko,

Uraji Misugi,

Iwabuchi Masaki,

Hatanaka Tadashi

Publication year - 2006

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2006.01.014

Subject(s) - streptomyces griseus , aminopeptidase , biochemistry , enzyme , calcium , chemistry , streptomyces , biology , leucine , stereochemistry , amino acid , genetics , bacteria , organic chemistry

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 ( p NA) and a decrease in that toward Lys‐ p NA. 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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