Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases

V.A. Money; N.L. Smith; Adrian Scaffidi; Robert Stick; H.J. Gilbert; G.J. Davies

doi:10.1002/anie.200600802

Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases

V.A. Money, N.L. Smith, Adrian Scaffidi, Robert Stick, H.J. Gilbert, G.J. Davies

School of Molecular Sciences

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

Abstract

Pick-a-path: A series of enzymatic snapshots along the reaction coordinate of a lichenase (specific for gluco-configured substrates) demonstrates that this enzyme uses a different reaction pathway, featuring a 1S3→4H3→4C1 migration, to that previously observed for the closely related mannanases.

Original language	English
Pages (from-to)	5136-5140
Journal	Angewandte Chemie (International Edition)
Volume	45
Issue number	31
DOIs	https://doi.org/10.1002/anie.200600802
Publication status	Published - 2006

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10.1002/anie.200600802

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title = "Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases",

abstract = "Pick-a-path: A series of enzymatic snapshots along the reaction coordinate of a lichenase (specific for gluco-configured substrates) demonstrates that this enzyme uses a different reaction pathway, featuring a 1S3→4H3→4C1 migration, to that previously observed for the closely related mannanases.",

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AU - Stick, Robert

AU - Gilbert, H.J.

AU - Davies, G.J.

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AB - Pick-a-path: A series of enzymatic snapshots along the reaction coordinate of a lichenase (specific for gluco-configured substrates) demonstrates that this enzyme uses a different reaction pathway, featuring a 1S3→4H3→4C1 migration, to that previously observed for the closely related mannanases.

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DO - 10.1002/anie.200600802

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ER -

Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases

Abstract

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