Sandbox Reserved 1077

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.

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Rv0045c hydrolase from M. TuberculosisRv0045c hydrolase from M. Tuberculosis

Function

Disease

Relevance

Structural highlights

The of this enzyme is typical of α/β hydrolases

The structure solved by x-ray crystallography^[1] was missing the 37 residues as well as a (residues 194-204). A theoretical FALC-loop model for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204^[2].

ReferencesReferences

↑ Zheng X, Guo J, Xu L, Li H, Zhang D, Zhang K, Sun F, Wen T, Liu S, Pang H. Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLoS One. 2011;6(5):e20506. Epub 2011 May 26. PMID:21637775 doi:10.1371/journal.pone.0020506
↑ Lukowski JK, Savas CP, Gehring AM, McKary MG, Adkins CT, Lavis LD, Hoops GC, Johnson RJ. Distinct substrate selectivity of a metabolic hydrolase from Mycobacterium tuberculosis. Biochemistry. 2014 Dec 2;53(47):7386-95. doi: 10.1021/bi501108u. Epub 2014 Nov, 17. PMID:25354081 doi:http://dx.doi.org/10.1021/bi501108u

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OCA, Geoffrey C. Hoops

[1] Zheng X, Guo J, Xu L, Li H, Zhang D, Zhang K, Sun F, Wen T, Liu S, Pang H. Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLoS One. 2011;6(5):e20506. Epub 2011 May 26. PMID:21637775 doi:10.1371/journal.pone.0020506

[2] Lukowski JK, Savas CP, Gehring AM, McKary MG, Adkins CT, Lavis LD, Hoops GC, Johnson RJ. Distinct substrate selectivity of a metabolic hydrolase from Mycobacterium tuberculosis. Biochemistry. 2014 Dec 2;53(47):7386-95. doi: 10.1021/bi501108u. Epub 2014 Nov, 17. PMID:25354081 doi:http://dx.doi.org/10.1021/bi501108u

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