Crystal Structure of the Pyrococcus horikoshii Isopropylmalate Isomerase Small Subunit Provides Insight into the Dual Substrate Specificity of the Enzyme

2004 ◽  
Vol 344 (2) ◽  
pp. 325-333 ◽  
Author(s):  
Yoshiaki Yasutake ◽  
Min Yao ◽  
Naoki Sakai ◽  
Tomomi Kirita ◽  
Isao Tanaka
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Small Subunit ◽  
Pyrococcus Horikoshii ◽  
Dual Substrate Specificity ◽  
Insight Into ◽  
Dual Substrate

scholarly journals Dual-substrate Specificity Short Chain Retinol Dehydrogenases from the Vertebrate Retina

2002 ◽  
Vol 277 (47) ◽  
pp. 45537-45546 ◽  
Author(s):  
Françoise Haeseleer ◽  
Geeng-Fu Jang ◽  
Yoshikazu Imanishi ◽  
Carola A. G. G. Driessen ◽  
Masazumi Matsumura ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Short Chain ◽  
Vertebrate Retina ◽  
Dual Substrate Specificity ◽  
Dual Substrate

scholarly journals The crystal structure of mycobacterial epoxide hydrolase A

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Eike C. Schulz ◽  
Sara R. Henderson ◽  
Boris Illarionov ◽  
Thomas Crosskey ◽  
Stacey M. Southall ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Drug Targets ◽  
Epoxide Hydrolase ◽  
Sequence Similarity ◽  
Structural Similarity ◽  
High Sequence Similarity ◽  
High Structural Similarity ◽  
Potential Drug Targets ◽  
Insight Into

Abstract The human pathogen Mycobacterium tuberculosis is the causative agent of tuberculosis resulting in over 1 million fatalities every year, despite decades of research into the development of new anti-TB compounds. Unlike most other organisms M. tuberculosis has six putative genes for epoxide hydrolases (EH) of the α/β-hydrolase family with little known about their individual substrates, suggesting functional significance for these genes to the organism. Due to their role in detoxification, M. tuberculosis EH’s have been identified as potential drug targets. Here, we demonstrate epoxide hydrolase activity of M. thermoresistibile epoxide hydrolase A (Mth-EphA) and report its crystal structure in complex with the inhibitor 1,3-diphenylurea at 2.0 Å resolution. Mth-EphA displays high sequence similarity to its orthologue from M. tuberculosis and generally high structural similarity to α/β-hydrolase EHs. The structure of the inhibitor bound complex reveals the geometry of the catalytic residues and the conformation of the inhibitor. Comparison to other EHs from mycobacteria allows insight into the active site plasticity with respect to substrate specificity. We speculate that mycobacterial EHs may have a narrow substrate specificity providing a potential explanation for the genetic repertoire of epoxide hydrolase genes in M. tuberculosis.

scholarly journals Correction: Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity

PLoS ONE ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. e0190844
Author(s):  
Seoung Min Bong ◽  
Kka-bi Son ◽  
Seung-Won Yang ◽  
Jae-Won Park ◽  
Jea-Won Cho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Structural Basis ◽  
Related Protein ◽  
Insight Into
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