Professional Documents
Culture Documents
in
http://www.biochemden.in/biochemistry-analysis-questions/
1. Provide a reasonable systematic name for an enzyme that catalyzes the following
reaction:
fructose + ATP > fructose-1 phosphate + ADP
2. The IUBMB has a developed a set of rules for classifying enzymes based upon the type of
reaction they catalyze. The classification scheme assigns an Enzyme Commission (EC)
number to each enzyme. Answer the following questions regarding EC numbers and the class
of reaction catalyzed:
(a) What name is associated with class 4 enzymes and what type of reaction do they
catalyze?
(b) Oxidoreductases catalyze redox reactions. What class of enzymes are
oxidoreductases?
(c) What types of reactions are catalyzed by ligases?
3. There are many mechanisms that enzymes utilize to enhance reaction rates. Explain how
the following mechanisms enhance reaction rates:
(a) Covalent catalysis
(b) Proximity effects
4. List four characteristics that define a metabolic pathway.
5. Identify two amino acids that commonly act as nucleophiles in enzyme catalyzed
reactions.
6. What is the difference between an (1) isomerization reaction and (2) a rearrangement?
7. Enzyme catalyzed reactions that make or break C-C bonds typically involve carbanion
intermediates. One means of stabilizing a carbanion intermediate involves the formation of a
Schiffs base. Draw a strcuture of :
(a) a Schiffs base carbanion
(b) the resonance stabilized Schiffs base in the ene-amine form
8. How can metabolic inhibitors be used to determine the sequence of reactions in a
metabolic pathway?
9. Isotopes of C, N, S, P and H have been extensively used to investigate metabolic
pathways. Why?
10. The standard transformed free energy change for the following bimolecular reaction:
Glucose + ATP -> Glucose-6-phosphate + ADP
is -16.7 kJ/mol. Consequently, this reaction is spontaneous under standard conditions. Under
what conditions would this reaction NOT be spontaneous at 298K?
Solutions:
1. Fructose:ATP phosphotransferase or Fructose:ATP kinase
2. (a) Lyases catalyze group eliminations that form double bonds
(b) Class 1
(c) Bond formation coupled to ATP hydrolysis.
3. (a) Covalent catalysis enhances reaction rates by breaking down an overall reaction into at least two
elementary reaction steps. In particular, the E a (activation energy) for each of elementary steps is smaller
than the Ea (activation energy) associated with the single step reaction. The mechanism is referred to as
covalent catalysis as a covalent enzyme:substrate intermediate is formed and broken during the overall
reaction.
(b) Proximity effects enhance reaction rates by forcing the reacting groups to be near to one another in
space. This increases the rate at which the reacting groups encounter one another and increases the rate
of product forming reactions.
4. Metabolic pathways are (1) irreversible, (2) have a committed step, (3) are regulated and
(4) catabolic and anabolic pathways differ.
5. Serine, threonine and cysteine are nucleophilic in their ionized form, while histidine and lysine are
nucleophiles in their neutral-charged form.
6. Isomerization reactions inevitably involve the movement of an H atom without changing the
backbone while rearrangements involve changes to the carbon backbone.
carbon