M1. CLINICAL CHEMISTRY SEASON 2

BIOLOGIC PROTEIN THAT CATALYZES BIOCHEMICAL REACTIONS

BIOLOGIC PROTEIN THAT CATALYZES BIOCHEMICAL REACTIONS

ENZYME

THESE ARE PRODUCED BY THE CELLS TO SPEED UP THE REACTION OF A SPECIFIC ORGANIC MATTER

INTRACELLULAR PROTEINS

TRUE OR FALSE. ENZYMES ARE NOT NORMALLY HIGH IN THE PLASMA/SERUM, IN THE BLOOD, ENZYME LEVEL IS LOW. THIS IS WHY WHEN ENZYME IN THE BLOOD INCREASES, THIS IS ASSOCIATED WITH ABNORMALITIES.

A. BOTH ARE TRUE

B. BOTH ARE INCORRECT

C. 1ST FALSE, 2ND TRUE

D. 1ST TRUE, 2ND FALSE

A

INCREASED ENZYME LEVELS IN THE BLOOD MAY BE DUE TO?

CELL INJURY/DAMAGE, INCREASED MEMBRANE PERMEABILITY

THIS DISEASE CAUSES AN INCREASE IN ALT IN THE PLASMA

LIVER DISEASE

IN THE LABORATORY, HOW ARE ENZYMES MEASURED?

BASED ON ITS ACTIVITY

TRUE OR FALSE. THE CONCENTRATION OF ENZYME AFFECTS ITS ENZYMATIC REACTION (DIRECTLY PROPORTIONAL)

TRUE

THE HIGHER THE ENZYME REACTION, THE __ ITS CATALYTIC MECHANISM

FASTER

AS A BIOCATALYST, ENZYMES ARE AFTER THE __ OF THE CHEMICAL REACTION TO PRODUCE A PRODUCT

VELOCITY

TRUE OR FALSE. ENZYMES ARE THEN CONSUMED OR ALTERED AFTER THE CHEMICAL REACTION UPON PRODUCING A PRODUCT

FALSE

THE BRANCH OF SCIENCE THAT DEALS WITH THE STUDY OF PHYSICAL AND CHEMICAL PROPERTIES OF ENZYMES, ITS FUNCTIONS, AND ITS CLINICAL APPLICATION

ENZYMOLOGY

WATER LESS CAVITY WHERE SUBSTRATES BIND

ACTIVE SITE

WHEN A SUBSTRATE BIND TO THE ACTIVE SITE, IT WILL UNDERGO WHAT?

CHEMICAL REACTION

TRUE OR FALSE. ACTIVE SITE IS ALWAYS SPECIFIC TO THE SUBSTRATE

TRUE

IN ORDER FOR A SUBSTRATE TO BIND TO THE ACTIVE SITE, THE SUBSTRATE MUST CONFORM TO THE __ OF THE CAVITY

SHAPE

DIFFERENCE IN SHAPE OF A SUBSTRATE AND OF THE CAVITY MAY RESULT TO?

NO BINDING

WATER LESS CAVITY OTHER THAN THE ACTIVE SITE THAT BINDS REGULATORY OR EFFECTOR MOLECULES

ALLOSTERIC SITE

SUBSTANCES ACTED UPON BY ENZYMES, ALWAYS SPECIFIC FOR A PARTICULAR TYPE OF ENZYME

SUBSTRATES

THESE ARE NON-PROTEIN ENTITIES THAT IS ADDED TO THE ENZYME SUBSTRATE-COMPLEX TO ENHANCE ENZYME ACTIVITY

COFACTORS

THIS IS ALSO KNOWN AS THE SECOND SUBSTRATE

COENZYME

AN ORGANIC SUBSTANCE THAT HASTENS OR SPEEDS UP ENZYMATIC ACTIVITY

COENZYME

COENZYME IS FREQUENTLY USED IN WHAT TYPE OF ACTIVITY?

OXIDOREDUCTASE

HOW WOULD YOU KNOW IF THE ENZYME IS OXIDOREDUCTASE?

WHEN THE ENZYME ENDS WITH “DH”

LACTATE DEHYDROGENASE IS AN EXAMPLE OF WHAT ACTIVITY?

OXIDOREDUCTASE

NAD, NADH, NADP AND NADPH ARE EXAMPLES OF?

COENZYME

NAD:

A. OXIDIZED FORM

B. REDUCED FORM

A

NADH:

A. OXIDIZED FORM

B. REDUCED FORM

B

IF NAD IS THE PRODUCT, HOW TO MEASURE NAD

DECREASED ABSORBANCE IS MEASURED AT 340 NM

IF NADH IS THE PRODUCT, HOW TO MEASURE NADH

INCREASED ABSORBANCE IS MEASURED AT 340 NM

USUALLY METALLIC IONS, SOMETIMES NONMETALLIC, THAT IS ADDED TO THE ENZYME TO ENHANCE THE ENZYME-SUBSTRATE BINDING

ACTIVATOR

AN EXAMPLE OF NONMETALLIC ACTIVATOR ARE?

CHLORIDE AND BROMIDE

AN EXAMPLE OF METALLIC ACTIVATOR ARE?

MAGNESIUM, CALCIUM, ZINC, AND IRON

ENZYMES WITH SIMILAR ENZYMATIC ACTIVITY BUT DIFFER IN THE PHYSICAL, CHEMICAL, AND IMMUNOLOGIC CHARACTERISTICS

ISOENZYME

CREATININE KINASE (CK/CPK) IS AN EXAMPLE OF?

ISOENZYME

THESE THREE ENZYMES HAS THE SAME CATALYTIC ACTIVITY BUT DIFFER WHEN SUBJECTED TO ELECTROPHORESIS AS IT HAS DIFFERENT MIGRATION CHARACTERISTICS

CK1, CK2, CK3

WHICH OF THE CK/CPK IS THE FASTEST TO MIGRATE AND THE CLOSEST TO THE ANODE?

CK1

WHICH OF THE CK/CPK IS SLOWEST TO MIGRATE AND FARTHEST TO THE ANODE

CK3

PROTEIN PROTION OF THE ENZYME—WHEN IT IS SUBJECTED TO DENATURATION, THE ENZYME MAY LOSE ITS FUNCTION

APOENZYME

WHAT STRUCTURE OF PROTEIN MUST BE ALTERED FOR DENATURATION TO OCCUR?

TERTIARY STRUCTURE

THIS IS RESPONSIBLE FOR THE PHYSICAL AND BIOCHEMICAL PROPERTIES OF PROTEIN AND ITS OVERALL FUNCTION

TERTIARY STRUCTURE

ACTIVE SUBSTANCE FORMED FROM THE COMBINATION OF A COENZYME AND AN APOENZYME

HOLOENZYME

COENZYME + APOENZYME =

HOLOENZYME

WHEN COENZYME IS TIGHTLY BOUND TO ENZYME, COENZYME BECOMES A?

PROSTHETIC GROUP

ENZYME NAMING WAS BASED ON?

ENZYME COMMISSION OF INTERNATIONAL UNION OF BIOCHEMISTRY

THIS IS THE LONG NAME OF THE ENZYME, DEFINES THE SUBSTRATE ACTED ON, THE REACTION CATALYZED AND POSSIBLY THE COENZYME INVOLVED

SYSTEMIC NAME

USEABLE OR THE TRIVIAL NAME OF THE ENZYME—THIS IS WHAT WE USE IN THE LABORATORY AND HOW BOOKS PRESENT ENZYMES

RECOMMENDED NAME

IN ENZYME COMMISSION NUMERICAL CODE, FIRST DIGIT IS THE?

ENZYME CLASSIFICATION

IN ENZYME COMMISSION NUMERICAL CODE, SECOND DIGIT IS THE?

ENZYME SUBCLASSIFICATION

IN ENZYME COMMISSION NUMERICAL CODE, THIRD DIGIT IS THE?

ENZYME SUB-SUBCLASSIFICATION

IN ENZYME COMMISSION NUMERICAL CODE, FOURTH DIGIT IS THE?

SPECIFIC SERIAL NUMBER OF THE ENZYME SUB-SUBCLASSIFICATION

WHAT CLASSIFICATION OF ENZYME IS SHOWN:

A- + B —> A + B-

OXIDOREDUCTASES

ENZYMES THAT CATALYZE REDOX REACTIONS BETWEEN TWO SUBSTRATES

OXIDOREDUCTASES

CLASSIFICATION OF ENZYME. MALATE DEHYDROGENASE

OXIDOREDUCTASES

CLASSIFICATION OF ENZYME. GLUTAMATE DEHYDROGENASE

OXIDOREDUCTASES

CLASSIFICATION OF ENZYME. G6PD

OXIDOREDUCTASES

WHAT CLASSIFICATION OF ENZYME IS SHOWN:

A-X + B —> A + B-X

TRANSFERASES

ENZYME THAT CATALYZE THE TRANSFER OF CHEMICAL GROUO, WHETHER ITS PHOSPHATE OR METHYL GROUP, OTHER THAN HYDROGEN BETWEEN TWO SUBSTRATES

TRANSFERASES

CLASSIFICATION OF ENZYME. ALANINE AMINOTRANSFERASE

TRANSFERASES

CLASSIFICATION OF ENZYME. ASPARTATE AMINOTRANSFERASE

TRANSFERASES

CLASSIFICATION OF ENZYME. CREATININE KINASE

TRANSFERASES

CLASSIFICATION OF ENZYME. AMYLASE

HYDROLASES

CLASSIFICATION OF ENZYME. LIPASE

HYDROLASES

CLASSIFICATION OF ENZYME. PHOSPHATASES

HYDROLASES

WHAT CLASSIFICATION OF ENZYME IS SHOWN:

ATP —> cAMP + PPi

LYASES

ENZYMES THAT CATALYZE THE REMOVAL OF GROUPS FROM SUBSTRATES WITHOUT HYDROLASES. IN ITS ACTIVITY, THE PRODUCT REMAINS TO CONTAIN DOUBLE BONDS

LYASES

CLASSIFICATION OF ENZYME. FRUCTOSE BIPHOSPHATE ALDOLASE

LYASES

WHAT CLASSIFICATION OF ENZYME IS SHOWN:

A —> B

ISOMERASES

ENZYMES THAT CATALYZE THE INTERCONVERSION OF THE GEOMETRIC, OPTICAL AND POSITIONAL ISOMERASE

ISOMERASES

THIS IS WHEN SUBSTRATE IS TRANSFORMED TO A DIFFERENT FORM

ISOMERASES

CLASSIFICATION OF ENZYME. TRIPHOSPHATE ISOMERASE (TPI)

ISOMERASES

WHAT CLASSIFICATION OF ENZYME IS SHOWN:

Ab + C —> A-C + B

LIGASES

ENZYMES THAT CATALYZE THE JOINING OF TWO SUBSTRATE MOLECULES COUPLED WITH THE BREAKING OF PYROPHOSPHATE BOND IN ATP.

LIGASES

CLASSIFICATION OF ENZYME. GLUTATHIONE SYNTHETASE

LIGASES

ENZYME CATALYZES PHYSIOLOGIC REACTIONS BY __ THAT THE REACTANT MUST REACH

LOWERING THE ACTIVATION ENERGY LEVEL

THIS IS THE ENERGY REQUIRED FOR THE REACTANTS TO PRODUCE A PRODUCT

ACTIVATION ENERGY LEVEL

IF THE ACTIVATION ENERGY REQUIRED IS HIGH, THE EXPECTED TIME OF THE REACTION IS?

PROLONGED

IF THE ACTIVATION ENERGY REQUIRED IS LOW, THE EXPECTED TIME OF REACTION IS?

FASTER

ARRANGE IN ORDER: RELATIONSHIP BETWEEN ENZYME SUBSTRATE AND PRODUCT:

A. SUBSTRATE WILL UNDERGO CONVERSION AND WILL CHANGE INTO A PRODUCT

B. ACTIVE SITE OF THE ENZYME WOULD BIND WITH SUBSTRATE

C. PRODUCT WILL BE RELEASED

D. ENZYMES REMAIN UNCHANGED AND ONLY INCREASES THE VELOCITY

B, A, C, D

ENZYMES COMBINE WITH ONLY ONE SUBSTRATE AND CATALYZE ONLY ONE CORRESPONDING REACTION (ONE ENZYME, ONE SUBSTRATE, ONE REACTION)

ABSOLUTE SPECIFICITY

ENZYMES COMBINE WITH ALL SUBSTRATES CONTAINING A PARTICULAR CHEMICAL GROUP

GROUP SPECIFICITY

KINASE COMBINES WITH SUBSTRATES CONTAINING WHAT GROUP?

PHOSPHATE GROUP

ENZYMES COMBINE TO SPECIFIC SUBSTRATES WITH SPECIFIC CHEMICAL BONDS

BOND SPECIFICITY

AMYLASE COMBINES WITH COMPLEX SUGAR WITH?

GLYCOSIDIC BONDS

ENZYMES COMBINE WITH ONLY ONE OPTICAL ISOMER

STEREOISOMETRIC SPECIFICITY

WITH THE AMOUNT OF ENZYME EXCEEDING THE AMOUNT OF SUBSTRATE, THERE WILL BE A STEADY INCREASE IN SUBSTRATE CONCENTRATION AS MORE SUBSTRATE IS ADDED

SUBSTRATE CONCENTRATION

IF THE ENZYME CONCENTRATION IS GREATER THAN THE SUBSTRATE CONCENTRATION, THERE WILL BE?

NO MEASURABLE ACTIVITY

WHEN THE CONCENTRATION OF TEST ANALYTE IS TOO HIGH, WHAT SHOULD BE DONE?

DILUTE THE SERUM

TRUE OR FALSE. WHEN SUBSTRATE REACHES THE MAXIMAL CONCENTRATION, ADDITION OF SUBSTRATE WILL CAUSE A RAPID REACTION

FALSE

TYPE OF SATURATION KINETICS WHEREIN THE REACTION RATE IS PROPORTIONAL TO THE SUBSTRATE CONCENTRATION

FIRST ORDER KINETICS

TRUE OR FALSE. IN FIRST ORDER KINETICS, THE HIGHER THE SUBSTRATE CONCENTRATION THAT WOULD REACT TO THE ENZYME, THE LOWER IS THE REACTION PRODUCT

FALSE

TYPE OF SATURATION KINETICS WHEREIN REACTION WOULD ONLY AFFIX NUMBER OF SUBSTRATE IN EXCESS

ZERO ORDER KINETICS

WHAT TYPE OF SATURATION KINETICS IS USED IN MEASUREMENT OF ENZYME ACTIVITY IN THE LABORATORY

ZERO ORDER KINETICS

TRUE OR FALSE. IN FIRST ORDER KINETICS, CONCENTRATION OF THE SUBSTRATE IS FIXED

FALSE

MORE ENZYME IS PRESENT, MORE AVAILABLE ACTIVE SITE FOR SUBSTRATE CONCENTRATIONS, THE FASTER THE PRODUCT FORMATION (DIRECTLY PROPORTIONAL)

ENZYME CONCENTRATION

MOST PHYSIOLOGIC ENZYMATIC REACTIONS OCCUR IN RANGE OF WHAT PH?

7.0-8.0

PLASMA PH?

7.35-7.45

AVERAGE ARTERIAL PH:

7.4