Most effective catalysts

(a)  

Two types of enzymes

(a)  

composed only of protein (amino acid chains)

(a)  

has a non-protein part in addition to a protein part

(a)  

protein part of a conjugated enzyme

(a)  

non-protein part of a conjugated enzyme

(a)  

the biochemically active conjugated enzyme

(a)  

haloenzyme is a combination of?

(a)  

small organic molecules or Inorganic ions

(a)  

two other names for Cofactors that are organic molecules:

(a)  

these are derived from dietary vitamins

(a)  

a type of cofactors having typical metal ion conductors

(a)  

enumerate the four typical metal ion under Inorganic Ion Cofactors (Example: Pb2+/Co2+/Sc2+/Au2+)

(a)  

An example of non-metallic ion cofactor

(a)  

the reactant in an enzyme-catalyzed reaction

(a)  

In the fermentation process sugar to be converted to CO2, what is the substrate

(a)  

Three important aspects of the naming process of enzymes

(a)  

Give an example of digestive enzymes that are exempted in suffix -ase

(a)  

often used in addition to the type of reaction

(a)  

Major class of enzyme for Oxidation-reductions

(a)  

Major class of enzyme for functional group transfer reactions

(a)  

Major class of enzyme for hydrolysis reactions

(a)  

Major class of enzyme for Reactions involving addition or removal of groups form double bonds

(a)  

Major class of enzymes for isomerization reaction

(a)  

Major class of enzymes for Reactions involving bond formation coupled with ATP hydrolysis

(a)  

requires a coenzyme that is either oxidized or reduced as the substrate in the reaction.

(a)  

an enzyme that catalyzes the transfer of a functional group from one molecule to another

(a)  

Two major subtype of Transferase

(a)  

A subtype of transferase enzyme catalyze transfer of an amino group to a substrate

(a)  

A subtype of transferase enzyme, catalyze transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate

(a)  

an enzyme that catalyzes a hydrolysis reaction

(a)  

A hydrolase enzyme that catalyzes the breakage of peptide linkages in proteins

(a)  

A hydrolase enzyme that catalyzes the breaking of ester linkages in triacylglycerols

(a)  

an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

(a)  

Two subtypes of Lyase enzyme

(a)  

A lyase that effects the removal of the components of water from a double bond

(a)  

a Lyase enzyme that effects effects the addition of the components of water to form a double bonds

(a)  

an enzyme that catalyzes the isomerization (rearrangement of atoms) reactions.

(a)  

enzyme that catalyzes the formation of a bond between two molecules involving ATP hydrolysis

(a)  

Relatively small part of an enzyme’s structure that is actually involved in catalysis

(a)  

Place where substrate binds to enzyme

(a)  

Formed due to and bending of the protein.

(a)  

shape of enzyme active site

(a)  

Needed for the activity of enzyme

(a)  

Model of substrate binding that states that Enzyme has a predetermined shape for the active site

(a)  

Model of substrate binding that states that Only substrate of specific shape can bind with active site

(a)  

a substrate binding to enzyme model that states that Substrate contact with enzyme will change the shape of the active site

(a)  

Forces that determine substrate binding

(a)  

ENZYME SPECIFICITY that states that An enzyme will catalyze a particular reaction for only one substrate

(a)  

ENZYME SPECIFICITY that is the most restrictive of all species

(a)  

Example of Enzyme with absolute specificity

(a)  

ENZYME SPECIFICITY that states An enzyme can distinguish between stereoisomers.

(a)  

ENZYME SPECIFICITY that states that it Involves structurally similar compounds that have the same functional groups

(a)  

Example of Group Specificity

(a)  

ENZYME SPECIFICITY that states that it involves a particular type of bond irrespective of the structural features in the vicinity of the bond

(a)  

ENZYME SPECIFICITY that is Considered most general of enzyme specificities

(a)  

Example of Linkage Specificity

(a)  

4 factors that affects enzyme activity

(a)  

Temperature at which the rate of enzyme catalyzed reaction is maximum.

(a)  

Optimum temperature for human enzyme in degrees C.

(a)  

pH at which enzyme has maximum activity

(a)  

Optimum pH of PEPSIN

(a)  

Optimum pH of Trypsin

(a)  

At a constant enzyme concentration, the enzyme activity increases with increased_

(a)  

the concentration at which it reaches its maximum rate and all of the active sites are full

(a)  

Number of substrate molecules converted to product per second per enzyme molecule under conditions of optimum temperature and pH

(a)  

At a constant substrate concentration, enzyme activity increases with increase in_

(a)  

a substance that slows down or stops the normal catalytic function of an enzyme by binding to it.

(a)  

Compete with the substrate for the same active site

(a)  

(a)   inhibitors will have similar charge & shape

Do not compete with the substrate for the same active site

(a)  

a site where noncompetitive inhibitors binds to the enzyme at a location other than active site

(a)  

when a competitive inhibitor binds to an enzyme active site, the inhibitor remains unchanged

(a)  

a competitive inhibition with weak bonds

(a)  

if inhibitor concentration is greater than substrate concentration, the inhibitor dominates the occupancy process. What type of competitive inhibition?

(a)  

a competitive inhibition that can be reduce by simply increasing the concentration of the substrate

(a)  

What type of non-competitive inhibition? A noncompetitive enzyme inhibitor decreases enzyme activity by binding to a site on an enzyme other than the active site

(a)  

What type of non-competitive inhibition? ➔ Causes a change in the structure of the enzyme and prevents enzyme activity.

(a)  

What type of inhibition --> An enzyme inhibitor inactivates enzymes by forming a strong covalent bond with the enzyme's active site.

(a)  

an enzyme inhibition where Enzyme is permanently inactivated.

(a)  

Two binding sites of allosteric enzymes:

(a)  

Binding of substrate to allosteric site can lead to change in enzyme activity, if the regulators increase the enzyme activity, it is called?

(a)  

Binding of substrate to allosteric site can lead to change in enzyme activity, if the regulators decrease the enzyme activity, it is called?

(a)  

If an activator increases the enzyme activity, what type of control it is?

(a)  

If an inhibitor decreases the enzyme activity, what type of control it is?

(a)  

A process in which activation or inhibition of the first reaction in a reaction sequence is controlled by a product of the reaction sequence.

(a)  

Enzymes in inactive form

(a)  

If there is a removal of peptide fragment in a zymogen, it will be called (a)   which is the active form?

1st general Mechanism involved in enzyme regulation

(a)  

2nd General Mechanism in Enzyme Regulation

(a)  

3rd general mechanism in enzyme regulation

(a)  

A process in which enzyme activity is altered by covalently modifying the structure of the enzyme

(a)  

Most common covalent modification is the addition or removal of (a)   group

removal of the phosphate (phosphorylation) is catalyzed by a (a)  

Addition of the phosphate (phosphorylation) is catalyzed by (a)  

a prodrug that is activated when phosphate group is added

(a)  

Enzyme that catalyzes that addition of phosphate group in acyclovir to activates it

(a)  

In covalent modification of enzymes, phosphate group is added or remove in the R-group of what 3 amino acids

(a)  

an active product of addition of three phosphate groups to acyclovir is called?

(a)  

A prodrug that requires removal of phosphate group to activate it.

(a)  

The active form of a prodrug Fosphenytoin when phosphate group is removed by phosphatase

(a)  

substance that kills bacteria or inhibits their growth

(a)  

an enzyme that is an octa-peptide hormone, responsible for blood pressure regulation by narrowing blood vessels

(a)  

ACE-inhibitors block the action of ACE which converts (a)   to angiotensin

Person to discover sulfa drugs which is a collective term for drugs containing sulfanilamide

(a)  

Sulfanilamide is structurally similar to (a)   which acts as a competitive inhibitors of it.

Many bacteria need PABA to produce coenzyme (a)  

competitive inhibitor of enzymes responsible for converting PABA to folic acid in bacteria

(a)  

Sulfanilamides specifically inhibit the enzyme (a)   which will convert PABA to Folic acid

first discovered prodrug, and once undergoes acid reduction, it will form Sulfanilamide

(a)  

use synergistically with sulfanilamide

(a)  

An enzyme that is being inhibited by Trimethoprim

(a)  

a drug containing sulfanilamide being combine with Trimethoprim

(a)  

A drug which is a combination of Sulfamethoxazole and Trimethoprim

(a)  

Enzyme inhibited by Cotrimoxazole

(a)  

Accidently discovered by Alexander Fleming in 1928

(a)  

Penicillins have structures containing a four-membered ___ fused with a five-membered ___

(a)  

Selectively inhibits transpeptidase by covalent modification of serine residue

(a)  

catalyzes the formation of peptide cross links between polysaccharides strands in bacterial cell walls

(a)  

An enzyme which makes the bacteria resistant to Penicillins

(a)  

Three parts of Penicillin

(a)  

a cell wall synthesis inhibitor which inhibits cell wall synthesis through inhibition of the enzyme transpeptidase

(a)  

Synthetic anti-bacterial agent which will inhibit DNA topoisomerase and DNA-gyrase

(a)  

the best broad-spectrum antibiotics because it is effective against skin and bone infections as well as against infections involving the urinary, gastrointestinal, and respiratory systems

(a)  

It is the drug of choice for treatment of traveler’s diarrhea

(a)  

Biochemical threats associated with terrorism has thrust into the spotlight because this drug is effective against anthrax

(a)  

component of grapefruit juice which makes it an enzyme inhibitor

(a)  

most important enzyme for diagnosis of diseases

(a)  

Activates the enzymes plasminogen → plasmin (activated). When activated, this enzyme dissolves blood clots in the heart and often provides immediate relief.

(a)  

Fibrinolytic agents often combines with streptokinase

(a)  

A test for kidney malfunction by detecting the amount of ammonia present in blood which indicates the amount of urease enzyme

(a)  

Organic compounds, essential in small amounts for the proper functioning of the human body, must be obtained from dietary sources because the body cannot synthesize it.

(a)  

Year of Discovery of Thiamin (B1)

(a)  

Year of Discovery of Vitamin A

(a)  

Year of Discovery of Vitamin B2 (Riboflavin), C (Ascorbic Acid), and D (Sunshine Vitamin)

(a)  

Year of Discovery of Vitamin E

(a)  

Year of Discovery of Vitamin B12

(a)  

Year of Discovery of Vit K

(a)  

Year of Discovery of Vit B5 (Panthothenic acid), and B7 (Biotin)

(a)  

Year of Discovery of Vit B6 (Pyridoxine, Pyridoxal, Pyridoxamine)

(a)  

Year of Discovery of Vitamin B3 (Niacin, Nicotinic acid, Nicotinamide)

(a)  

Year of Discovery of Vitamin B9 (Folate)

(a)  

First vitamin to discovered

(a)  

A disease where vitamins reach high toxic levels

(a)  

Vitamin with simplest structure and acquired through breastmilk

(a)  

amount of vitamin C that saturates all body tissues in mg/day

(a)  

Maximum intake of Vit C in mg

(a)