What would happen to the concentrations of the compounds if a substance were add
ID: 1069688 • Letter: W
Question
What would happen to the concentrations of the compounds if a substance were added that inhibits the enzyme that catalyzes Y rightarrow Z? The concentrations of W and X would be higher, but the concentrations of Y and Z would be lower. The concentrations of W and X would be lower, but the concentrations of Y and Z would be higher. The concentrations of Z would be lower and all other concentrations would be nearly the same. The concentrations of W and X would be nearly the same, the concentrations of Y would be higher, and the concentrations of Z would be lower. The concentrations of all compounds would approach zero. Recall that pH-rate profiles provide information about ionizable groups that are within an enzyme active site and involved in catalysis and/or substrate binding. Considering the pH-rate profile shown to the right, which statement is MOST LIKELY true? Only one ionizable group is present within the active site. A lysine side chain acts as a nucleophile and an aspartate side chain in its protonated form binds a substrate. A glutamate side chain interacts with a positively-charged substrate and a histidine side chain acts as a general acid. The optimal pH for this enzyme is 7.0. A glutamate side chain acts as a general acid and a histidine side chain acts as general base. Consider the following scheme relevant to our study of enzyme kinetics: E + S Equilibrium ES rightarrow E + P Which of the following statements must be CORRECT? A competitive inhibitor would bind to ES A mixed inhibitor would only bind to E [P] NestedLessLess [S]Explanation / Answer
q 13
A glumate side chain interact with positively charged substrate and histidine side chain act as a general acid
Electrostatic interactions :
Substrates containing ionisable practical gatherings which are charged in watery arrangement or close ph 7 are regularly bound by means of electrostatic cooperations to oppositively charged amino corrosive side chain at the compound dynamic site.
Carboxylic acis (Pka =4.5) are found as contrarily charged anion at ph 7 and all the more decidedly charged side chain, for example, protonated aminoacid side chain of lysine .
Emphatically charged substrate gatherings can be bound electrostatically ot contrarily charged aminaocid side chains of gluatamine.
A reactant set of three charge-transfer framework as usually found in proteases.
The corrosive buildup (ordinarily glutamate or aspartate) adjusts and captivates the base (normally histidine) which actuates the nucleophile (frequently serine or cysteine, sometimes threonine).
The group of three decreases the pKa of the nucleophilic buildup which then assaults the substrate.
An oxyanion gap of emphatically charged for the most part spine amides(occasionally side-chains) settle energize expand on the substrate move state.
The base is most ordinarily histidine since its pKa takes into consideration successful base catalysis, hydrogen attaching to the corrosive deposit, and deprotonation of the nucleophile buildup. -lactamases, for example,
TEM-1 utilize a lysine deposit as the base. Since lysine's pKa is so high (pKa=11), a glutamate and a few different buildups go about as the corrosive to settle its deprotonated state amid the synergist cycle.
Related Questions
drjack9650@gmail.com
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.