Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB),-Reference-Cited by-同舟云学术

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Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB),

Published:2010-01-22 Issue:6 Volume:49 Page:1082-1092
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nguyen Henry H.¹,Wang Liangbing²,Huang Hua²,Peisach Ezra³,Dunaway-Mariano Debra²,Allen Karen N.¹³

Affiliation:

1. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2394

2. Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131

3. Department of Chemistry, Boston University, Boston, Massachusetts 02215

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi902019q

Reference39 articles.

1. Observation of Covalent Intermediates in an Enzyme Mechanism at Atomic Resolution

2. Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: Mechanistic implications

3. Catalytic activity of rabbit skeletal muscle aldolase in the crystalline state.

4. Trapping intermediates in the crystal: ligand binding to myoglobin

5. Enzymatic transition states: thermodynamics, dynamics and analogue design

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2. Experimental and computational analysis of the ancestry of an evolutionary young enzyme from histidine biosynthesis;Protein Science;2022-12-29

3. A thermophilic phosphatase from Methanothermobacter marburgensis and its application to in vitro biosynthesis;Enzyme and Microbial Technology;2022-09

4. Pathogen-Associated Molecular Patterns: The Synthesis of Heptose Phosphates and Derivatives;Synthesis;2021-09-06

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