(Q35084343)

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A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Europe PubMed Central

A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases (English)

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Nerinckx W

1

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Europe PubMed Central

PubMed publication ID

6 August 2017

Desmet T

2

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Europe PubMed Central

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6 August 2017

Claeyssens M

3

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Europe PubMed Central

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6 August 2017

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1 March 2003

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Europe PubMed Central

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6 August 2017

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Europe PubMed Central

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6 August 2017

538

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6 August 2017

1-3

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Europe PubMed Central

PubMed publication ID

6 August 2017

1-7

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Structural and sequence-based classification of glycoside hydrolases

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STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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Glycosidase mechanisms

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Enzymatic catalysis as a process controlled by protein conformational relaxation.

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Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase

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Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state

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X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies

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The Pfam protein families database

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Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei

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Identifiers

10.1016/S0014-5793(03)00148-0

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

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