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Biochemistry, Biophysics, and Structural Biology Commons™
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- Chem_stsc (3)
- Biochemistry (2)
- Biol_stsc (2)
- Malate dehydrogenase (2)
- Citric acid cycle (1)
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- E. coli (1)
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- Enzyme catalysis (1)
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- Galactooligosaccharides (GOS) (1)
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- Metabolism (1)
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- Non-Canonical Amino Acid (1)
- Prebiotics (1)
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- Recombinant protein engineering (1)
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Articles 1 - 4 of 4
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Site-Directed Mutagenesis Of Malate Dehydrogenase: A Class Project, Bruce J. Heyen, Chesley Rowlett, Jon Zatorski, Ryan Burch, Emily Veach, Andy Gemmaka
Site-Directed Mutagenesis Of Malate Dehydrogenase: A Class Project, Bruce J. Heyen, Chesley Rowlett, Jon Zatorski, Ryan Burch, Emily Veach, Andy Gemmaka
Scholar Week 2016 - present
Malate dehydrogenase (MDH) is an important enzyme in an organism’s metabolic pathways. MDH is found in almost all living cells and catalyzes the conversion of malate to oxaloacetate which also involves nicotinamide dehydrogenase (NAD) as a coenzyme. A method to study how an enzyme operates is to alter one of its amino acids and compare the activity of the enzyme before and after the mutation. As a class project in Advanced Biochemistry during the spring semester of 2018, we are working as a team to propose and carry out a point-based mutation on MDH.
Effect Of An Arginine-To-Isoleucine Active Site Mutation On Escherichia Coli Malate Dehydrogenase Enzymatic Activity, Jon Zatorski, Bruce J. Heyen
Effect Of An Arginine-To-Isoleucine Active Site Mutation On Escherichia Coli Malate Dehydrogenase Enzymatic Activity, Jon Zatorski, Bruce J. Heyen
Scholar Week 2016 - present
Citric acid cycle enzymes function in an environment with numerous substrate analogues and therefore contain active site residue organizations that confer high substrate specificity. Extensive research into the catalytic mechanism of Escherichia coli malate dehydrogenase (eMDH) has identified arginine81 as being crucial to catalysis. In this investigation, an engineered eMDH having an Ile81 rather than an Arg81 (R81I) was isolated using a hexahistadine (His6) tag. Enzymatic activity of the R81I mutant with respect to malate, lactate, and pyruvate was explored. The R81I mutant did show significant activity toward malate, but did not show significant activity toward lactate or pyruvate. Investigations …
Synthesis And Incorporation Of 1,2-Alkanolamine-Functionalized Lysine As A Non-Canonical Amino Acid Into Gfp, Chesley M. Rowlett
Synthesis And Incorporation Of 1,2-Alkanolamine-Functionalized Lysine As A Non-Canonical Amino Acid Into Gfp, Chesley M. Rowlett
Scholar Week 2016 - present
Synthesis of specific post translational modifications in proteins can be difficult but achievable via genetic code expansion techniques. An attempt has been made to synthesize and incorporate D-cThrK into green fluorescent protein (GFP) at an amber mutation site in Escherichia coli via the coordination of pyrrolysyl- tRNA synthetase and its cognate tRNApyl. The incorporation of this non-canonical amino acid and potential chemical transformations following it allow the synthesis of proteins with post translational lysine modifications, making a variety of basic and biotechnological applications available.
The Effects Of Inulin And Galactooligosaccharides On The Production Of Reuterin By Lactobacillus Reuteri, Micah Forshee
The Effects Of Inulin And Galactooligosaccharides On The Production Of Reuterin By Lactobacillus Reuteri, Micah Forshee
Scholar Week 2016 - present
The microbiome is a dynamic community that can positively and negatively influence host health. Lactobacillus reuteri is a probiotic that has received much attention for its ability to inhibit pathogens such as Salmonella Typhimurium, Escherichia coli, and Clostridium difficile. It does so by its unique ability to metabolize glycerol into the antimicrobial compound 3-HPA, which is commonly referred to as reuterin. The ability to secrete reuterin is dependent not only on glycerol availability but also the concentration of glucose. In fact, there appears to be a “goldilocks” ratio between glucose and glycerol as either too much or too …