Flashcards in Biochem Deck (51):
What are organic compounds that activate enzymes showing Michaelis Menten kinetics called? Examples?
Cofactors, eg Mg+
What equation is equal to pH?
Describe the quaternary structure bonding of a protein
Requires bonds to form between the side chains of the amino acids that are part of two separate protein molecules. The type of bonds formed are the same as those formed in the tertiary structure.
Side chain of CYSTEINE
Side chain of ALANINE
Side chain of ASPARTIC ACID
Side chain of SERINE
Side chain of LYSINE
Stages between a keratin molecule and a keratin filament
1 a-keratin molecule
5 a-keratin filament
What groups are attached to the centra carbon atom in an amino acid?
What are the most abundant proteins in muscle?
Actin and myosin
How many katals of enzyme activity is the amount required to catalyse the conversion of 1 mole of a substrate to the product in 1 second?
In the presence of a competitive inhibitor is the km increased, decreased or unchanged?
In the presence of a competitive inhibitor is the Vmax increased, decreased or unchanged?
How does temperature affect the activity of an enzyme reaction?
Name two properties of competitive inhibitors
They can be overcome by increasing the substrate concentration.
They have a similar shape to the substrate.
Name a competitive inhibitor
Name a non-competitive inhibitor
Name an irreversible inhibitor
Name an inhibitor that acts as a nerve poison (irreversible)
Name two properties of irreversible inhibitors
They usually prevent the substrate entering the active site.
They usually bond to the side chain of either serine or cysteine at the enzyme active site.
Name two properties of allosteric enzymes
They show sigmoidal rather than hyperbolic (Michaelis Menten) kinetics.
They must contain two or more sub-units.
How does a change in the pH affect bonding in enzymes?
Effect the electrostatic (ionic) bonding in the tertiary structure of enzymes
Is the -OH group in a-glucose above or below the ring?
Which types of glycosidic bond are found in glycogen?
When a -NH2 group replaces an -OH group it is called _________
When a -COOH group replaces the -OH group on C6 it is called __________
When an -H replaces an -OH group it is called _______
Why does cellulose form long straight chains?
Because every alternate glucose unit inverts
What molecules unbranched and highly branched molecules are starch made up of?
What are the names for a carbon atom with 4 different atoms or groups attached to it by a covalent bond?
What are functions of carbohydrates?
Which of the following monosaccharides are the components of lactose?
What carbonyl groups are found in monosaccharides?
What is the most abundant protein in most vertebrates?
What is the Km?
What is the michaelis constant?
An indication of the affinity of an enzyme for it's substrate
At ____ concentrations of a substrate, the rate of an enzyme reaction is directly proportional to the substrate concentration if the concentration of the enzyme remains constant.
Cellulose forms long straight chains because every alternate glucose unit _______
What is a common non-reducing disaccharide?
What is an epimer?
An isomer of a monosaccharide where the only difference is the side of the central carbon backbone that the -OH and -H point on one carbon atom only
Which type of glycosidic bond is found in cellulose?
Name the polysaccharide found in bacterial cell walls
What is the protein in muscle which binds to and acts as a store of oxygen
Which of the following is the polysaccharide found in insect exoskeletons?
What is the name of the enzyme that converts pyruvate to lactate?
What does alchohol dehydrogenase convert acetylaldehyde to?
What toxic substance does alcohol dehydrogenase catalyse the conversion of methanol to
Which enzyme catalyses the major control point in glycolysis?
How many molecules of ATP are produced form ADP by substrate level phosphorylation when glucose is converted to pyruvate by glycolysis?