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Covalent catalysis is used by many enzymes to cleave peptide bonds .
Which amino acid would not facilitate this type of catalysis? - --
<<answer>>--Valine, because nonpolar AA lacks nucleophile to facilitate
generation of catalyst-substrate covalent bond.
T/F Heme is not a coenzyme - --<<answer>>--True
Ligases are a class of enzyme characterized by its ability to: - --
<<answer>>--synthesize bonds between carbon atoms and additional
atom that is involved in clevage of high energy bond.
Activity of an enzyme is increased when enzyme is phosphorylated on
exposed tyrosine residue. Phosphorylation of this amino acid is
classified as: - --<<answer>>--Covalent modification.
Enzyme inhibitor increases Km, but does not change Vmax - --
<<answer>>--Competitive inhibitor
, Cleavage of fructose 1, 6 biphosphate to dihydoxyacetone and
glyceraldehyde 3 phosphate is achieved by what class of enzyme? - --
<<answer>>--Lypase.
Movement of ammonia from amino acid to alpha keto acid involves
family of enzymes categorized as: - --<<answer>>--Transferases
Competitive inhibitor competes with a substrate for binding at enzyme
active site. This interaction causes which of the following changes in
enzyme activity? - --<<answer>>--Addition of competitive inhibitor will not
impact Vmax of enzyme.
What is OH concentration in a 0.01 M (10^-2) solution of HCl? - --
<<answer>>--([OH]= 10^-14/0.1 M) 10^-12
Enzymes facilitate reactions through this mechanism - --<<answer>>--
Decrease activation energy
Enzyme regulation through covalent modification - --<<answer>>--
phosphorylation of muscle glycogen phosphorylase
Tyrosine is an aromatic acid with pKa of 10.5. At physiological 7.4, what
is charge of R group? - --<<answer>>--Neutral.