The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?
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The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?
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- A biochemical reaction will proceed in the direction as written if: Group of answer choices H > 0. G = zero. H G > 0. GWhich one is the most likely to be a catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-AlaDIY Glue State the materials that use to make it. Show the mechanisms of the reaction that occur.
- True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.Enzyme modification by chemical procedures affecting amino acid side chainsThe use of co-factors in catalysis : 3.1 Metal-activated enzymes and metalloenzymes definition for each term 3.2 Cofactors Cofactor Origin Structure Catalytic role Nicotinamide nucleotides Flavin nucleotides Adenosine phosphates Coenzyme A Biotin Coenzyme B12 Summaries the characteristics of co-factors using this table. Use both the textbook and other online sources such as Wikipedia to find the information. Under origin, report the precursor molecule e.g. “niacin” and also try to find the Vitamin X name for each compound, e.g. “Vitamin B3”. Under structure, identify the unique structural properties that allow each cofactor to perform the function it does Under catalytic role, indicate for which reactions are each of the cofactors important
- SaccharidesCatalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysisMechanisms of catalysis: 2.3 Covalent catalysis summary + example
- A member of the staff at the care home inquires about paracetamol with the pharmacist. This employee requested to purchase 4 boxes of paracetamol (each having 16 pills), but the grocer refused. What is the reason behind this? Please provide a biochemical explanation. please make the answer longProtease is an enzyme that catalyzes the breaking of amide bonds which is very stable at “mild” conditions, namely body temperature and pH 7 (if done in the lab requires hot conditions, concentrated HCl for hours). Some proteases have two aspartic acid residues at their active sites. Write the reaction mechanism (which follows general acid-base catalysis)Mechanisms of catalysis: 2.4 Enzymen catalysis summary