Question

in the reaction that is catalyzed by isocitrate lyase, what mechanisms are employed to achive catalysis...

in the reaction that is catalyzed by isocitrate lyase,
what mechanisms are employed to achive catalysis (acid-base, covalent, nuceolphilic, etc?), what are the cofactor and intermediates in the reaction?
Science   Biology   
0 0
Add a commentTranscribed image text
Next >

Homework Answers

Answer #1

Isocitrate lyase is an enzyme (composed of four identical chains) which catalyzes the reaction where isocitrate is broken into succinate and glyoxylate. This is an oxo-acid lyase enzyme and this enzyme acts on C-C bonds. In the reaction catalyzed by ICL, isocitrate is deporotonated first and then an aldol cleavage occurs. This reaction produce sucinate and glyoxylate.

The reaction mechanism is shown below:

Mg2+ or Mn2+ and a thiol acts as cofactors for Isocitrate lyase enzyme.

0 0
Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Log In

Sign Up

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
Give a brief description of fructose 1,6 bisphosphate aldolase. In what pathway does the enzyme occur?...
Give a brief description of fructose 1,6 bisphosphate aldolase. In what pathway does the enzyme occur? What reaction does the enzyme catalyze? What type of reaction is catalyzed? What are the intermediates in the reaction? What are the cofactors? What mechanisms are employed to achieve catalysis (acid-base, covalent, nucleophilic, etc???) What type of regulation controls the activity of the enzyme?
Phosphorylation of glucose by hexokinase illustrates which kind of enzyme reaction mechanism? (a) covalent catalysis (b)...
Phosphorylation of glucose by hexokinase illustrates which kind of enzyme reaction mechanism? (a) covalent catalysis (b) proximity and positioning (c) general acid-base catalysis (d) metal ion catalysis/redox (e) none of the above
Which of the following is NOT a mechanism employed by enzymes to lower the energy of...
Which of the following is NOT a mechanism employed by enzymes to lower the energy of the transition state? High substrate binding affinity ? General acid/base catalysis? Metal ion catalysis ? Covalent catalysis ? Proximity and orientation effects?
What is the difference between H2SO4 and H3O+ in acid catalyzed hydration reaction?
What is the difference between H2SO4 and H3O+ in acid catalyzed hydration reaction?
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if...
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if it were carried out in a 0.1 M buffer initially at pH 6.63, and 0.003 M of acid was produced during the reaction? (The buffer used was a polyprotic acid of the general form: H3A; the three pKas of this polyprotic acid are 2.06, 6.63, and 11.30.)
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if...
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if it were carried out in a 0.1 M buffer initially at pH 6.66, and 0.004 M of acid (H+) was produced during the reaction? (The buffer used was a polyprotic acid of the general form: H3A; the three pKas of this polyprotic acid are 2.16, 6.66, and 11.23.)
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if...
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if it were carried out in a 0.1 M buffer initially at pH 2.07, and 0.005 M of acid (H+) was produced during the reaction? (The buffer used was a polyprotic acid of the general form: H3A; the three pKas of this polyprotic acid are 2.07, 6.56, and 11.22.) (The enzyme's normal environment is the stomach.)
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if...
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if it were carried out in a 0.1 M buffer initially at pH 2.07, and 0.004 M of acid (H+) was produced during the reaction? (The buffer used was a polyprotic acid of the general form: H3A; the three pKas of this polyprotic acid are 2.07, 6.7, and 11.37.) (The enzyme's normal environment is the stomach.)
1. What is the rate-limiting, regulated enzyme in glycolysis? 2. Draw the complete reaction catalyzed by...
1. What is the rate-limiting, regulated enzyme in glycolysis? 2. Draw the complete reaction catalyzed by this enzyme with the structures of the glycolytic intermediates (substrates or products coming directly from glucose) 3. Draw an idealized Vo vs [S] plot for this enzyme. On the graph, identify and show the effect of the major allosteric inhibitor of this enzyme in muscle. Also identify and show the effect of the major allosteric activator of this enzyme in muscle.
Can you show me what this reaction looks like: Ribulose bisphosphate carboxylase, RuBP (Photosynthesis, Calvin cycle,...
Can you show me what this reaction looks like: Ribulose bisphosphate carboxylase, RuBP (Photosynthesis, Calvin cycle, stage I) full reaction with reactants, intermediates, final products, acid/base, water
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT