Enzymes

Question 1

Enzymes

Answer 1

Specific proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition

Question 2

Catalyze the transfer of a group other than hydrogen from one substrate to another

Answer 2

Transferases

Question 3

Catalyze the interconversion of geometrix, optical, or positional isomers

Answer 3

Isomerases

Question 4

Catalyze removal of groups from substrates without hydrolysis; the product contains double bonds

Answer 4

Lyases

Question 5

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bond in adenosine triphosphate or a similar compound

Answer 5

Ligases

Question 6

A constant for a specific enzyme and substrate under defined reaction conditions and can provide an expression of the relation between he velocity of an enzymatic reaction and substrate concentration

Answer 6

Michaelis-Menten constant (Km)

Question 7

Elevated in disorders of cardiac and skeletal muscle (myocardial infarction, rhabdomyolysis, and muscular dystrophy)

Answer 7

Creatinine Kinase

Question 8

Catalyzes the interconversion of lactic and pyruvic acids, transfer enzyme that uses the coenzyme NAD+

Answer 8

Lactate dehydrogenase

Question 9

______ use with the production of ATP which results in relatively constant levels of muscle ATP, the reversible reaction catalyzed by CK

Answer 9

Creatinine phosphate

Question 10

Incorporates a coupled enzymatic reaction using malate dehydrogenase as the indicator reaction to monitor the change in absorbance at 340 nm continuously as NADH is oxidized to NAD+

It is a transaminase involved in the transfer of an amino acid between aspartate and a-keto acids

Answer 10

Aspartate Amino transferase

Question 11

It primarily evaluates hepatic disorders and catalyzes transfer of amino group from alanine to a-ketoglutarate with the formation of glutamate and pyruvate

Answer 11

Alanine aminotransferase

Question 12

Catalyze the hydrolysis of various phosphomonoesters at an alkaline pH

Answer 12

Alkaline phosphatase

Question 13

Uses the same techniques as in ALP assays but performed at an acid pH

Answer 13

Acid phosphatase

Question 14

Enzyme which uses enzymatic activity where the y-glutamyl residue to transfer to glycylglycine in order to release p-nitroaniline

Answer 14

y-Glutamyltransferase

Question 15

Enzyme activity for 5’-Nucleotidase

Answer 15

Catalyzes the hydrolysis of inosine monophosphate to inosine and free inorganic phosphate

Question 16

Catalyze the breakdown of starch and glycogen

Answer 16

Amylase

Question 17

Hydrolyzes the ester linkages of fats to produce alcohols and fatty acids from triglycerides

Answer 17

Lipase

Question 18

Uses pentose-phosphate shunt of glucose metabolism with the ultimate production of NADPH

Answer 18

Glucose-6-Phosphate Dehydrogenase

Question 19

Forms of plasma enzymes that are bound to an immunoglobulin or a nonimmunoglobulin substances

Answer 19

Macroenzymes

Question 20

Transform xenobiotics into active, water-soluble compounds for excretion through the kidneys

Answer 20

Drug-Metabolizing Enzymes

Question 21

Reference range for Lipase

Answer 21

<38 U/L (37C)

Question 22

Reference range for Alanine aminotransferase

Answer 22

7-45 U/L

Question 23

Referance range for Creatinine kinase

Answer 23

Male: 46-171 U/L
Female: 34-145 U/L

CK-MB: <5% total CK