Johns Hopkins UniversityProgram in Molecular Biophysics
Krisna Duong-LyAmzel Lab, Biophysics & Biophysical Chemistry

Krisna Duong-Ly

Class of 2005
krisna@jhu.edu

B.A. Biochemistry, Swarthmore College

Research
Serine racemase converts L-serine to D-serine, which has been implicated in normal neuronal migration and synaptic transmission as well as in pathological conditions such as schizophrenia and neurodegenerative damage accompanying stroke. Serine racemase also produces pyruvate through an elimination reaction. Despite the importance of D-serine, the mechanism of this bifunctional enzyme is still poorly understood. My research in this system focuses on investigating the structure, function, and mechanism of the serine racemase from Mus musculus.

In another project, I am studying a CDP-choline pyrophosphatase (CDP-Case) from Bacillus cereus. B. cereus is a food pathogen that is closely related to B. anthracis, the pathogen that causes anthrax. CDP-Case is a member of the Nudix superfamily of proteins. Nudix enzymes are those that hydrolyze the phosphoanhydride bond of “nucleoside diphosphates linked to some other moiety x.” CDP-Case hydrolyzes CDP-choline to produce CMP and phosphocholine, a component of phospholipid head groups. By studying the structure and mechanism of this enzyme, I hope to learn more about the physiology of B. cereus as well as to understand more about the mechanisms of Nudix enzymes.

Publications
Duong-Ly, K.C., V. Nanda, W.F. DeGrado, and K.P. Howard. (2005) The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14:856-861. PMID: 15741338

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