Mechanistic study of Glycolysis Hydrolase family 4 (GH4) enzyme with aim for industrial scale biocatalyst development and single particle cryo-EM based structural studies on co-translational protein modification in human
Dr. Samar Ballabha Mohapatra, Postdoctoral Research Scholar, Dept. of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, USA
Location : Online
Abstract: Mechanistic study of GH4 enzyme with aim for industrial scale biocatalyst development
The Glycolysis Hydrolase family 4 (GH4) are unique hydrolases, which harness the catalytic proficiency of Metalloenzymes (Mn2+ dependent) and Oxidoreductases (NAD+ dependent) to hydrolyze the glycosidic linkage. During my PhD at Professor, N. Manoj’s laboratory at IIT Madras, we have delineated the catalytic dehydration of substrate para Nitrophenol-α-Glucuronic acid (pNP-α-GlcA) by NAD+, releasing pNP and forming an α, β-unsaturated ketone (Michael acceptor) at the active site. This α, β- unsaturated ketone undergoes rehydration by the onboard NADH to give rise product GlcA, both of which, we have trapped in a ternary complex crystal structure. This transient Michael acceptor like chemical species indicates the reaction’s larger scope to be redirected towards catalytic conversion of carbon dioxide to formic acid and enzymatic glycoprotein synthesis.
Structural studies of mechanism of co-translational protein modification in human.
During my ongoing postdoctoral fellowship at Professor Ronen Marmorstein’s laboratory at the University of Pennsylvania, we are fishing out ribosomes from mammalian cell line using affinity tagged post translational modifying protein as bait for single particle cryo-EM based structural study.
Meeting ID: 914 9236 7434
Passcode: 623382
The Glycolysis Hydrolase family 4 (GH4) are unique hydrolases, which harness the catalytic proficiency of Metalloenzymes (Mn2+ dependent) and Oxidoreductases (NAD+ dependent) to hydrolyze the glycosidic linkage. During my PhD at Professor, N. Manoj’s laboratory at IIT Madras, we have delineated the catalytic dehydration of substrate para Nitrophenol-α-Glucuronic acid (pNP-α-GlcA) by NAD+, releasing pNP and forming an α, β-unsaturated ketone (Michael acceptor) at the active site. This α, β- unsaturated ketone undergoes rehydration by the onboard NADH to give rise product GlcA, both of which, we have trapped in a ternary complex crystal structure. This transient Michael acceptor like chemical species indicates the reaction’s larger scope to be redirected towards catalytic conversion of carbon dioxide to formic acid and enzymatic glycoprotein synthesis.
Structural studies of mechanism of co-translational protein modification in human.
During my ongoing postdoctoral fellowship at Professor Ronen Marmorstein’s laboratory at the University of Pennsylvania, we are fishing out ribosomes from mammalian cell line using affinity tagged post translational modifying protein as bait for single particle cryo-EM based structural study.
Meeting ID: 914 9236 7434
Passcode: 623382