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Article

A mutant alpha-amylase with enhanced activity specific for short substrates.

FEBS letters - 5 Oct 1992

Matsui I, Ishikawa K, Miyairi S, Fukui S, Honda K

Abstract excerpt

The 210th lysine (K210) at the active site in Saccharomycopsis fibuligera alpha-amylase was altered to arginine (R) or asparagine (N) by site-directed mutagenesis. Replacement of K210 by R strengthened the 7th and weakened the 8th subsite affinities. K210 was found to contribute to both the 8th and the 7th subsites. The catalytic activity of the K210R enzyme for the hydrolysis of maltose (G2) was three-times...

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Identifiers

PMID: 1397275
DOI: 10.1016/0014-5793(92)81335-j

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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