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Biochemistry 3381A Enzymes Midterm Summary.docx

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Department
Biochemistry
Course
Biochemistry 3381A
Professor
Brian Shilton
Semester
Fall

Description
Summary of Enzymes for Midterm #2 Enzyme Substrate Residues Type of More? Catalysis RNAase RNA and H O2 Resting state of enzyme: 2 Acid/base Basic His attacks the 2’ OH and Hydrolyzes histidines involved; one acting hydrolysis using the acidic His breaks the RNA as acid, one acting as a base 2 His residues phosphodiester His – NH+ His – N: Phosphoryl 2 phosphoryl transfer reactions transfer *His can act as A or B depending on microenvironment Aldolase Fructose 1,6 Lys acts as a nuc; normally Acid/base Lys forms Schiff base bisphosphate +vely charged. This Lys has to Covalent Asp deprotonates, breaks sugar (F16P) and be in an environment that H2O decreases pKa, to be neutral. Lys – N: Asp – O- Carbonic CO 2 Metalloenzyme Carbon dioxide comes in, OH anhydrase H O His Metal ion attacks then attaches and 2 - catalysis becomes bicarbonate. Catalyzes CO 2 - Lewis acid: Zn2+ Zn stabilizes OH- @ start of rxn + H2O → His llllllllll Zn2+ lllllllllll OHLewis base: OH- and favors formation of HCO - + H + - bicarbonate (HCO -) 3 3 - Water deprotonated by “proton His relay” with the histidines; until OH is generated Lysozyme Carbohydrate Glu – OH should be anion @ Acid/base D sugar is in half chair Lysozyme pH 7 but enzyme has formed Covalent b/c we conformation, different cleaves b/w microenvironment to cause it have a covalent conformation than other rings DNAM & to be in protonated form intermediate which is how enzyme recognizes ENAG its D ring is planar Asp – O- negatively charged Transition state is planar like we would normally expect carbocation which is what enzyme favors (favors binding to TS) D ring has the most free E; puts strain on
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