Lost lots of points. I want to know what I did wrong on this so I can prepare fo
ID: 176654 • Letter: L
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Lost lots of points. I want to know what I did wrong on this so I can prepare for finals. Please answer this in full details the more information the better so I can grasp it and learn.
Michaelis Menten pl Student animals. Both catalyze expressed two different of hexokinase are in versions el same enzymatic main of storage i catalyzed In the space reaction you glycogen in by below, learned about metabolism of the cell. and the significance of that reaction for the nase IV (liver) nce ntr hon Hexokinase (lil Celis And relati Mat mwn reel tien rotes hich Glucose Concentration (mM) Ind ts half of Vmax se concert lat -n. d) 6 pts. Based your evaluation of the Michaelis Menten plots, what conclusions can you make about the kinetic activities of ese hexokinase enzymes? For full credi you shoul estimate the Vmax and Km each and explain what each of those parameters "tells us about the enzyme and its activity. are find ther ractreh love at hexakinas ir Give Gymnaarira (vee se concentra both te rattfin made TA ch te hex kin se (tire has sense liv J e) 3 pts. Based on your understanding of the importance of this e nzyme in celular metabolism, explain why the difference in kinetic 8ctMy for these two versions of .maRes logical8ense. In other abou animal as a why does it nse bexRbDas body cells. that hexakinase IV in iver would have these kinetic properties compared to the p operties of the hexok found in other inase hoxokino. remove Its trying m enter y your body j tt AlsoExplanation / Answer
(C) Your writing is not clear enough to make me check and tell you about your mistakes..so i am providing you the answers....
1. Hexokinase catalyzes: glucose + ATP glucose-6-phosphate + ADP
The Hexokinase reaction involves nucleophilic attack of the C6 hydroxyl oxygen of glucose on the phosphorous of the terminal phosphate of ATP.
ATP binds to the enzyme as a complex with Mg++.
The positively charged Mg++interacts with negatively charged phosphate oxygen atoms of ATP, providing charge compensation and promoting a favorable conformation of ATP at the active site.
The reaction catalyzed by Hexokinase is highly spontaneous. A phosphoanhydride bond of ATP (~P) is cleaved. The phosphate ester formed in glucose-6-phosphate has a lower DG of hydrolysis.
Glucose binding to Hexokinase stabilizes a conformation in whichThe C6 hydroxyl of the bound glucose is close to the terminal phosphate of ATP, promoting catalysis.Water is excluded from the active site. This prevents the enzyme from catalyzing ATP hydrolysis, rather than transfer of phosphate to glucose.
It is a common motif for an enzyme active site to be located at an interface between protein domains that are connected by a flexible hinge region. The structural flexibility allows access to the active site, while permitting precise positioning of active site residues, and in some cases exclusion of water, as substrate binding promotes a particular conformation.
(D) Hexokinase has a much higher affinity for glucose than glucokinase. It is not about number of glucose molecules metabolized, or about energy of activation, vmax or induction. Km signifies the affinity of the enzyme for its substrate.
Km and its significance :-
° The michaelis constant km is the substrate concentration at which vi is the half the maximal velocity (vmax/2) attainable at a particular concentration of enzyme.
° it is specific and constant for a given enzyme under defined conditions of time, temperature and PH
° km determines the affinity of an enzyme for its substrate, lesser the km more is the affinity and vice versa.
° km value helps in determining the true substrate for the enzyme.
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