Structural Flexibility Enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning Its Mechanism of Hydrolysis-Reference-Cited by-同舟云学术

Structural Flexibility Enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning Its Mechanism of Hydrolysis

Published:2009-08-04 Issue:33 Volume:131 Page:11900-11908
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hadler Kieran S.¹,Mitić Nataša¹,Ely Fernanda¹,Hanson Graeme R.¹,Gahan Lawrence R¹,Larrabee James A.¹,Ollis David L.¹,Schenk Gerhard¹

Affiliation:

1. School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland, 4072, Australia, Centre for Magnetic Resonance, The University of Queensland, St. Lucia, Queensland, 4072, Australia, Department of Chemistry and Biochemistry, Middlebury College, Middlebury, Vermont 05753, and Research School of Chemistry, Australian National University, Canberra, ACT, 0200, Australia

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja903534f

Reference45 articles.

1. Enzymatic Mechanisms of Phosphate and Sulfate Transfer

2. Structure and function of the methionine aminopeptidases

3. The Catalytic Mechanisms of Binuclear Metallohydrolases

4. Binuclear Metallohydrolases

5. Metallo-β-lactamases: Novel Weaponry for Antibiotic Resistance in Bacteria

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