Flashcards in Biochemistry Deck (44)
How do catalysts function?
They speed up reaction rate be lowering the activation energy
What is the transition state (intermediate) in a reaction?
This is the unstable stage between reactants and products
What is the glycogen storage disease and what are its consequences?
It is an enzyme deficiency that results in the failure of glycogen to reach the phosphorylated state.
This means glucose cannot be obtained from glycogen stores
Hepatomegaly(fatty liver) will result due to glycogen build up
What are the variants of the extra molecules (as well as enzymes) that often required for some enzymatic processes to proceed?
Cofactors- metal ions
Coenzymes- organic molecules
What are the metal ions that contain metal cofactors called?
Like enzymes, cofactors are always ______ at the end of a reaction
Tightly bound coenzymes are called what?
Prosthetic groups (these have additional functions)
What is the term given to an enzyme without a cofactor?
An enzyme with a cofactor is called what?
Give examples of metal ions that could be used as cofactors
Give examples of coenzymes
Binding of a substrate to an enzyme results in what?
Conformational change of the enzyme around the substrate
This is induced fit (due to intermolecular bonding)
The enzyme/substrate complex is now formed
Which two main factors affect enzyme functionality?
Describe how temperature can affect the rate of an enzymatic reaction
It will increase to a point and the sharply drop off (past the optimum temp) due to enzyme denaturing
Describe how increasing pH affect the rate of an enzymatic reaction
It will increase as pH increases until the optimum rate is achieved (at optimum pH) and will then decrease again
This produces a bell curve
What are isozymes?
Enzymes which have almost identical function but have slightly different amino acid sequencing
How can the number of certain isozymes in certain tissues/blood be used to diagnose a medical condition?
Different isozymes are synthesised in different regions of the body or at different stages in embryonic/foetal development
Finding the "wrong" isoenzyme at a certain time, or location in the body may be indicative of a medical condition
How can phosphorylation regulate enzyme activity?
It can convert the enzyme between inactive and active forms
Phosphorylation is a reversible process that involves which two enzymes?
1. Kinase- adds phosphate
2. Phosphatase- removes phosphate
What are zymogens?
Inactive precursors of an enzyme which are converted to active forms by cleavage of a covalent bond
What is produced after the catabolism of glucose?
Two pyruvate molecules
There is also a net gain of 2ATP, 2NADH and 2H+
What is NAD+?
Nicotinamide adenine dinucleotide
It is derived from niacin- a vitamin
It is used as an electron carrier by forming NADH
What is NADH required for?
The transfer of electrons to the respiratory electron transfer chain in stage 3 of ATP synthesis
What are the three different terms used to describe the second stage of ATP synthesis?
1. Citric acid cycle
2. Krebs cycle
3. Tricarboxylic acid cycle (TCA)
Where does the TCA cycle occur?
Mitochondrial matrix on the inner membrane
(this is where proteins required for the electron transport chain can be found, as well as ATP synthase and transport proteins
Where is pyruvate synthesised?
How does pyruvate enter the matrix of the mitochondria (3)?
It must cross two membranes
- The intermembrane space is very acidic creating a pH gradient from the cytosol to the matrix which pyruvate can follow
-There is also a electrochemical gradient and pyruvate can utilise this as it is attracted to H+
- A pyruvate symport transporter allows entry of pyruvate into the mitochondria using H+/pyruvate symport, a form a con transport, by facilitated diffusion
Which process must pyruvate undergo to be converted yo acetyl-CoA?
This is an irreversible reaction
Describe the 4 stages of the oxidative decarboxylation of pyruvate
1. Pyruvate dehydrogenase converts pyruvate to hydroxyethyl thiamine pyrophosphate (HETPP, CO2 is given off as a byproduct
2. Dihydrolipoyl transacetylase transfers( and oxidises) the hydroxyethyl group to lipoid acid which forms acetyl dihydrolipoamide
3. The acetyl group is transferred to CoA forming one acetyl CoA per pyruvate
4. NAD+ reoxidises dihydrolipoamide which forms one NADH- this is mediated by dihydrolipoyl