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Full-Text Articles in Physical Sciences and Mathematics
Characterization Of The Mala Enzyme From Bdellovibrio Bacteriovorus Through The Synthesis And Analysis Of Maltose Derivatives, Joey R. Jepson
Characterization Of The Mala Enzyme From Bdellovibrio Bacteriovorus Through The Synthesis And Analysis Of Maltose Derivatives, Joey R. Jepson
Summer Research
MalA is an α-glucosidase found in the bacterium Bdellovibrio bacteriovorus, a predatory bacteria that preys on gram-negative bacteria, including several plant and human pathogens. The gene for MalA was discovered while sequencing the genome of Bdellovibrio and was predicted to be a maltase based on homology. Maltase enzymes are characterized by their role in the catalysis of maltose into two glucose subunits. MalA will bind to several different disaccharides composed of a glucose α-linked to a variety of sugars (isomaltose, trehalose, turanose, sucrose, etc.), but it does not cleave them. The objective of our research was to investigate how the …
Synthesis Of A Lysozyme Substrate: Exploring The Use Of The (2,6-Dichloro-4-Methoxyphenyl)(2,4-Dichlorophenyl)) Methyl (Mdpm) Protecting Group In Glycoside Coupling, Vladimir Yelkhimov
Synthesis Of A Lysozyme Substrate: Exploring The Use Of The (2,6-Dichloro-4-Methoxyphenyl)(2,4-Dichlorophenyl)) Methyl (Mdpm) Protecting Group In Glycoside Coupling, Vladimir Yelkhimov
Summer Research
Hen egg white lysozyme and T4 lysozyme are two well-studied enzymes that have played an important role in helping us understand the structure and function of proteins. Both of these lysozymes function by breaking down cell walls. Although numerous studies on lysozyme catalysis have been conducted, detailed information on their substrate specificity has been lacking due to the heterogeneous nature of cell walls. The information we do have suggests that the T4 lysozyme cleaves only those oligosaccharides with an attached peptide chain while hen egg white lysozyme is less selective and will cleave oligosaccharides without peptide chains. I plan to …