Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase-Reference-Cited by-同舟云学术

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Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase

Published:2016-12-31 Issue:12 Volume:49 Page:681-686
ISSN:1976-6696
Container-title:BMB Reports
language:en
Short-container-title:BMB Reports

Author:

Tran Huyen-Thi,Lee Seon-Hwa,Ho Thien-Hoang,Hong Seung-Hye,Huynh Kim-Hung,Ahn Yeh-Jin,Oh Deok-Kun,Kang Lin-Woo

Publisher

Korean Society for Biochemistry and Molecular Biology - BMB Reports

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://ocean.kisti.re.kr/downfile/crosscheck/ksbmb/JAKO201606776011141.pdf

Reference24 articles.

1. Mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural Analysis of Reaction Intermediates

2. 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

3. Fructose-bisphosphate aldolases: an evolutionary history

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

5. Experimental Determination and System Level Analysis of Essential Genes in Escherichia coli MG1655

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1. The metal cofactor: stationary or mobile?;Applied Microbiology and Biotechnology;2024-06-24

2. Miniprotein-Based Artificial Retroaldolase;ACS Catalysis;2022-12-01

3. Substrate Induced Movement of the Metal Cofactor between Active and Resting State;Angewandte Chemie International Edition;2022-11-09

4. Substrate Induced Movement of the Metal Cofactor between Active and Resting State;Angewandte Chemie;2022-11-09

5. Fructuronate-tagaturonate epimerase UxaE from Cohnella laeviribosi has a versatile TIM-barrel scaffold suitable for a sugar metabolizing biocatalyst;International Journal of Biological Macromolecules;2020-11

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