Active Site Loop Dynamics of a Class IIa Fructose 1,6-Bisphosphate Aldolase from Mycobacterium tuberculosis-Reference-Cited by-同舟云学术

Active Site Loop Dynamics of a Class IIa Fructose 1,6-Bisphosphate Aldolase from Mycobacterium tuberculosis

Published:2013-01-18 Issue:5 Volume:52 Page:912-925
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Pegan Scott D.¹,Rukseree Kamolchanok²³,Capodagli Glenn C.¹,Baker Erica A.¹,Krasnykh Olga³⁴,Franzblau Scott G.³⁴,Mesecar Andrew D.⁵

Affiliation:

1. Eleanor Roosevelt Institute and Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado 80208, United States

2. National Center for Genetic Engineering and Biotechnology (BIOTEC), NSTDA, Thailand Science Park, Tha Khlong 12120, Thailand

3. Institute for Tuberculosis Research, University of Illinois at Chicago, Chicago, Illinois 60612, United States

4. Department of Medicinal Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States

5. Departments of Biological Sciences and Chemistry and Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300928u

Reference35 articles.

1. Fructose-bisphosphate aldolases: an evolutionary history

2. Structural Basis for Catalysis of a Tetrameric Class IIa Fructose 1,6-Bisphosphate Aldolase from Mycobacterium tuberculosis

3. Molecular cloning, expression, purification, and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis—a novel Class II A tetramer

4. The crystal structure of Escherichia coli class II fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity 1 1Edited by R. Huber

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