what is the covalent modification doing to the enzyme

Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level.  Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?

Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains.  Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How?  Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins

The natural enzyme is recreated by mixing isolated regulatory and catalytic subunits of ATCase. What biological relevance does this observation have?

A post doc was working on charaterizing a new enzyme and found that in a 357 amino acid enzyme, the amino acids 33,34,35 and amino acids 301,303,306 form one active site. Q1:As the PI, would you tell him 1) that this  result doesn't make any sense or 2) that this is a interesting finding? Explain your answer Q2: if the amino acid residues 33,34,35 were Phe,Val, and Ala, would this be possible to occur?

Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…

Most enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are structurally quite similar to one another. Why are highly specific enzymes advantageous from a biological perspective? They allow catalyzed reactions to produce potentially useful by-products. They allow for the sharing of enzymes by multiple metabolic pathways. They allow an inhibitor to simultaneously inhibit multiple steps in a metabolic pathway. They allow control of which reactions occur at appreciable rates. Why are most enzymes highly specific from a chemical perspective? Enzymes generally requires a tight fit between enzyme and substrate. Interactions between the enzyme and the substrate stabilize the substrate. The active sites of enzymes are always identical in shape to the substrates they bind. The formation of weak interactions between the enzyme and the substrate requires energy.

this is not a writing assignment or essay  just give a brief explanation

Is the data that you are collecting in the above table quantitative or qualitative? Explain why. Which treatment had the least amount of browning? Which had the most? Why do you think you obtained these results? Remember that the enzyme polyphenol oxidase is a protein! For each treatment, apply your knowledge of how temperature, pH, and salt concentration affect enzyme activity and explain why you got the results that you did. Include bonds and the levels of protein structure that you explored in Activity A in your answer. How does temperature impact the rate of enzyme activity? If you were to leave the apple in the refrigerator longer, why would it eventually brown? Explain based on what you know about enzyme activity. How does pH and its impact on specific types of bonds explain the results you obtained in your lemon juice treatment? Include bonds and levels of protein structure in your answer. How does salt and its impact on specific types of bonds explain the results you obtained…

Calculate 1/[S] and 1/V to complete the table. Use this data to draw a Lineweaver-Burke plot, with lines for ‘no inhibitor’ and ‘with inhibitor’. Be sure to label your axes and lines.  What kind of inhibitor is it? Estimate Vmax and Km for the uninhibited reaction.