L. Smyth scite author profile

L. Smyth

5Publications

78Citation Statements Received

30Citation Statements Given

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Affiliations

University of Victoria

Publications

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Analysis of Keystone Enzyme in Agar Hydrolysis Provides Insight into the Degradation (of a Polysaccharide from) Red Seaweeds

Hehemann

Smyth

Yadav

et al. 2012

Journal of Biological Chemistry

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Background:The catalytic mechanism and substrate recognition required for cleavage of the ␣-linkage in agarose are unclear.Results: Structural analysis of a family 117 glycoside hydrolase details substrate recognition and supports an inverting mechanism. Conclusion: GH117 enzymes use substrate distortion and an unusual general acid for catalysis. Significance: Microbes may utilize alternate strategies to catalyze the degradation of polysaccharides with unique structural characteristics.

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Crystal structure of protein AF1782 from Archaeoglobus fulgidus, Pfam DUF357

Bonanno¹,

Rutter²,

Bain³

et al. 2007

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Crystal structure of BpGH117_E303Q in complex with neoagarobiose

Hehemann¹,

Smyth²,

Yadav³

et al. 2012

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Native crystal structure of BpGH117

Hehemann¹,

Smyth²,

Yadav³

et al. 2012

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BpGH117_H302E mutant glycoside hydrolase

Hehemann¹,

Smyth²,

Yadav³

et al. 2012

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L. Smyth

Analysis of Keystone Enzyme in Agar Hydrolysis Provides Insight into the Degradation (of a Polysaccharide from) Red Seaweeds

Crystal structure of protein AF1782 from Archaeoglobus fulgidus, Pfam DUF357

Crystal structure of BpGH117_E303Q in complex with neoagarobiose

Native crystal structure of BpGH117

BpGH117_H302E mutant glycoside hydrolase

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