It increases availability of food for humans
The oceans store large amounts of energy
Answer:
The lock-and-key model:
c. Enzyme active site has a rigid structure complementary
The induced-fit model:
a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.
Common to both The lock-and-key model and The induced-fit model:
b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.
d. Substrate binds to the enzyme through non-covalent interactions
Explanation:
Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.
The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.
The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.
Answer:
CH₃CH₂-CH₂CH₃
Explanation:
When an alkene, R-CH=CH-R reacts with H₂ in a Pt catalyst, the analogue alkane, R-CH₂-CH₂-R, is produced (Hydrogenation of alkenes via Pt/Pd catalyst)
Thus, the reaction of CH₃CH=CHCH₃ with H₂ under a platinum catalyst produce:
<h3>CH₃CH₂-CH₂CH₃</h3>
The analogue alkane
