Proton
Enzymes use several types of catalytic mechanisms. Differentiate
between acid-base catalysis, covalent catalysis, and metal ion
catalysis.
Categorize these correctly
solution:
There are several differences of enzymes and use to catalyze specific reactions.
1. Covalent catalysis involves a an active site with a reactive group (substrate). The active site contains a reactive nucleophilic group that attacks the substrate through covalent forces. Although the covalent interactions are temporary, the substrate is bound to the enzyme during the course of catalysis. See mechanism of the proteloytic enzyme Chymotrypsin
for example of this strategy.
2. General acid-base catalysis involves acid base reactions that do not occur with water. Other molecules undergo proton accepting or donating.
3. Catalysis by approximation involves bringing two distinct substrates in close proximity which can increase the reaction rate considerably. See Nucleoside Monophosphate Kinase.
4. Metal ion catalysis involves metal ions that allow the formation of nucleophilles or electrophilles that can help the reaction occur in a faster pace.
the above are best study to which shows that one enzymes diffrence from one another
solution:
the below is the diffrence b/w catalysis
Proton
Acid = donates
proton, Enzyme active site must be protonated
Base = accepts proton, Enzyme active site must be
deprotonated
A covalent bond
is temporarily formed between the substrate and enzyme.
Both a nucleophile (enzyme) and an electrophile (substrate) are
involved.
Normally have a positive charge, unfilled electrons, or an EN atom
??Metalloenzymes - contain tightly bound metal cofactors (normally transition metals)Enzymes use several types of catalytic mechanisms. Differentiate between acid-base catalysis, covalent catalysis, and metal ion...
Are the following examples of general acid/base catalysis, covalent
catalysis, catalysis by approximation (proximity effect), or
metal-ion catalysis? Complete parts a, b, c, and d.
(b) NMP kinases bring two nucleotides, for example AMP and ATP,
together to facilitate the transfer of a phosphoryl group from one
nucleotide to the other (creating two ADP). The enzyme positions
the adenosine triphosphate (ATP) such that the gamma phosphate
group is placed adjacently to the phosphate group of the NMP
kinase. This facilitates...
1. Enzymes catalyze reactions by diverse mechanisms, frequently involving multiple steps. Consider the well-studied enzyme called chymotrypsin, which has three amino acids in its active site: Asp102, His 57, and Ser 195. What is the catalytic role of His 57? A. covalent catalysis B. general acid-base C. catalysis catalysis by approximation D. metal ion catalysis 2. Which of the following functional groups are not found in carbohydrates? A. aldehydes B. hydroxyls C. ketones D. thiols 3. What are the components...
D Which of the following is not one of the three most common catalytic reaction mechanisms in an enzyme active site? Choose one: A temporarily sharing electrons between two atoms B. protonation or deprotonation of an amino acid, or water, on the enzyme C. using the histidine side chain to form covalent bonds with the substrate D. utilizing positively charged metal ions to correctly orient the substrate, or to mediate redox reactions
(1-7). Shown below are the first steps of protein cleavage as catalyzed by chymotrypsin. The yellow cleft is the active site with side chains showing. Using this diagram, answer the following questions. Onyanion hole 07 1. This reaction involves what types of catalytic mechanisms: covalent catalysis general acid base catalysis metal catalysis A and B B and 5. What is false concerning the middle diagram of the active site shown above? It represents a transition state. Hydrogen bonds from the...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
PRE-LAB QUESTIONS 1. Differentiate between an acid and a base. 2. Calculate the pH and pOH of 1.2 x 10-3 M HCl solution. 3. Calculate pH, pOH and [OH-] of 0.1 M HNO3 solution. 4. If a solution X has pH = 5, which of the following is true: a. Solution X is neutral. b. H3O+ ion concentration is higher than OH- concentration. c. OH- ion concentration is higher than H3O+ concentration.
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...