PMID: 8444153Feb 15, 1993Paper

Effects of subsite alterations on substrate-binding mode in the active site of hen egg-white lysozyme

European Journal of Biochemistry
I KumagaiK Miura

Abstract

The subsite structures in the active site of hen egg-white lysozyme were altered by site-directed mutagenesis. Replacement of Trp62, which is involved in apolar interaction with a sugar ring, and Asp101, which is hydrogen bonded to the same sugar ring in subsite B, led to a shift of the oligosaccharide-binding mode in the active-site cleft. Consequently, the double-mutant lysozyme (Trp62His, Asp101Gly) exhibited a drastic change of substrate-binding without any significant loss of enzymic activity. Conversion of Asn37, which is postulated to be involved in interaction with a sugar ring in subsite F, had a reverse effect on substrate binding. Nuclear magnetic resonance analysis of mutant lysozymes, in which Trp62 was replaced with Phe or His, suggested that these replacements not only altered the structure of the amino acid chain at position 62 of the lysozyme, but also induced local structural changes around the residue at position 62.

References

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Citations

Oct 1, 1995·Protein Science : a Publication of the Protein Society·P Shih, J F Kirsch
May 29, 1998·Biochimica Et Biophysica Acta·K MaenakaI Kumagai
Feb 28, 2003·Biology of Reproduction·Arabinda MandalJohn C Herr
Apr 10, 2012·Bioscience, Biotechnology, and Biochemistry·Naoyuki UmemotoTamo Fukamizo
Jun 2, 2015·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Mami MatanoKenji Maehashi
Jun 29, 2005·Developmental Biology·María Belén HerreroJohn C Herr
Aug 5, 2010·Dalton Transactions : an International Journal of Inorganic Chemistry·Vincenzo AbbatePeter G Taylor
Sep 9, 2008·Journal of Biochemistry·Takashi GotoTadashi Ueda
Nov 9, 2019·International Journal of Molecular Sciences·Edward J TaylorKeith S Wilson

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