A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: Crystal structure and site-directed mutagenesis studies

2008 ◽  
Vol 1780 (5) ◽  
pp. 809-818 ◽  
Author(s):  
Taro Yamada ◽  
Junichi Komoto ◽  
Tatsuo Kasuya ◽  
Yoshimi Takata ◽  
Hirofumi Ogawa ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Activity ◽  
Cancer Cells ◽  
Catalytic Mechanism ◽  
Human Cancer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Human Cancer Cells ◽  
Serine Dehydratase

scholarly journals Catalytic Mechanism of Heparinase II Investigated by Site-directed Mutagenesis and the Crystal Structure with Its Substrate

2010 ◽  
Vol 285 (26) ◽  
pp. 20051-20061 ◽  
Author(s):  
David Shaya ◽  
Wenjing Zhao ◽  
Marie-Line Garron ◽  
Zhongping Xiao ◽  
Qizhi Cui ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Mechanism ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

A novel peroxisome proliferator-activated receptor α/γ agonist, BPR1H0101, inhibits topoisomerase II catalytic activity in human cancer cells

2008 ◽  
Vol 19 (2) ◽  
pp. 151-158 ◽  
Author(s):  
Yu-Hsun Kao ◽  
Hsing-Pang Hsieh ◽  
Santhosh Kumar Chitlimalla ◽  
Wen-Yu Pan ◽  
Ching-Chuan Kuo ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Cancer Cells ◽  
Topoisomerase Ii ◽  
Human Cancer ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Human Cancer Cells

Structural and biochemical analyses of theStreptococcus pneumoniaeL,D-carboxypeptidase DacB

2015 ◽  
Vol 71 (2) ◽  
pp. 283-292
Author(s):  
Juan Zhang ◽  
Yi-Hu Yang ◽  
Yong-Liang Jiang ◽  
Cong-Zhao Zhou ◽  
Yuxing Chen
Keyword(s):  
Crystal Structure ◽  
Molecular Docking ◽  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Binding Properties ◽  
Biochemical Analyses ◽  
Key Residues ◽  
Structural Insights

The L,D-carboxypeptidase DacB plays a key role in the remodelling ofStreptococcus pneumoniaepeptidoglycan during cell division. In order to decipher its substrate-binding properties and catalytic mechanism, the 1.71 Å resolution crystal structure of DacB fromS. pneumoniaeTIGR4 is reported. Structural analyses in combination with comparisons with the recently reported structures of DacB fromS. pneumoniaeD39 and R6 clearly demonstrate that DacB adopts a zinc-dependent carboxypeptidase fold and belongs to the metallopeptidase M15B subfamily. In addition, enzymatic activity assays further confirm that DacB indeed acts as an L,D-carboxypeptidase towards the tetrapeptide L-Ala-D-iGln-L-Lys-D-Ala of the peptidoglycan stem, withKmandkcatvalues of 2.84 ± 0.37 mMand 91.49 ± 0.05 s−1, respectively. Subsequent molecular docking and site-directed mutagenesis enable the assignment of the key residues that bind to the tetrapeptide. Altogether, these findings provide structural insights into substrate recognition in the metallopeptidase M15B subfamily.

Indirubin derivatives inhibit SFKs/Stat signaling associated with apoptosis in human cancer cells

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
S Nam ◽  
R Buettner ◽  
X Liu ◽  
J Turkson ◽  
D Kim ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Human Cancer ◽  
Human Cancer Cells ◽  
Stat Signaling
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