Structural Insights into the Substrate Binding and Stereoselectivity of Giardia Fructose-1,6-bisphosphate Aldolase,-Reference-Cited by-同舟云学术

Structural Insights into the Substrate Binding and Stereoselectivity of Giardia Fructose-1,6-bisphosphate Aldolase,

Published:2009-03-18 Issue:14 Volume:48 Page:3186-3196
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Galkin Andrey¹,Li Zhimin¹,Li Ling¹,Kulakova Liudmila¹,Pal Lipika R.¹,Dunaway-Mariano Debra¹,Herzberg Osnat¹

Affiliation:

1. W. M. Keck Laboratory for Structural Biology, Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, and Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9001166

Reference27 articles.

1. Functional role of metal ions in a class II aldolase

2. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase

3. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold

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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