Introduction

51問 • 1年前

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Biologic catalysts that cause reactions in the body to take place. These substance in the body increases the rate of chemical reaction.

ENZYME

Characterisitcs of enzymes are capable of ionizing either as acid or as a base

AMPHOTERIC

Use to define coenzyme

CO SUBSTRATE

Metabolic regulator of enzyme reaction

ACTIVATOR

the combined enzyme & coenzyme

HOLOENZYME

Acted upon by an enzyme & is converted into a new substance

SUBSTRATE

Substance derived from a transformed substrate

PRODUCT

Site other than the active site that may lead to either attachment of substrate to the enzymes

ALLOSTERIC SITE

Where an inhibitor or an activator can attach to

ACTIVE SITE

It inhibits the attachment of substrate to the active site

ALLOSTERIC INHIBITOR

These influences the enzyme particularly the sheath of active site.

ALLOSTERIC ACTIVATOR

Protein structure refering to the sequence of amino acids joined by peptide bonds to form a polypeptide chain

PRIMARY

Protein structure refering to conformation of the segments of polypeptide chain maintained by hydrogen bond. Samples are Alpha-helix; beta-pleated sheet

SECONDARY

Protein structure arises from the interactions among side chains/groups of the polypeptide chain. It is Bent and folded structure maintained by _______.

TERTIARY, COVALENT DISULFIDE BOND

Protein structure made up of 4 polypeptide units separated bended and folded structures are put together to form a functional unit.

QUARTERNARY

Assayed for investigation of cardiac and liver disorders

OXIDOREDUCTASE

Gives information about liver damage

TRANSFERASE

Splits molecules with water as part of the reaction process

HYDROLASE

Hydrolase 3 groups

ESTERASE, PEPTIDASE, GLYCOSIDASE

Responsible for splitting molecules or breaking of bonds (C to C; C to O; C to N, etc.) yielding two smaller articles from a large enzyme.

LYASE

Assayed in disorders of skeletal muscles

LYASE

Responsible for the conversion of one isomer to another

ISOMERASE

All reactions are reversible

ISOMERASE

Enzymes causing bond formation between two molecules to form larger molecule from two smaller molecules (in the presence of ligases) it became one large molecule

LIGASE

In-systematic naming of enzyme, the 1st digit denotes for

CLASS

In-systematic naming of enzyme, the 2nd digit denotes for

SUB CLASS

In-systematic naming of enzyme, the 3rd digit denotes for

SUBSUB CLASS

Multichained enzymes of similar activity. Appear in specific tissue, organ & cell organelle of similar organisms.

ISOENZYME

Lactate Dehydrogenase has how many isoenzyme

Isoenzyme of LDH found in heart, RBC & renal tubules

LDH1, LDH2

Isoenzyme of LDH found in liver, skeletal muscles

LDH4, LDH5

Enzymes that exert their function in plasma secreted by the liver

PLASMA SPECIFIC

Classification of enzyme found only in one location, particularly the cell sap (vacuoles of the cell the storage compartment of the cell which can store protein and sugar

UNILOCULAR ENZYME

Classification enzyme found in the Mitochondria & cell sap

BILOCULAR ENZYME

commonness between the enzyme and substrate

MOLECULAR COMPATIBILITY

the number of enzyme/substrates that can be reacted

SPACE AVAILABILITY

enzyme active on a specific substrate

SPECIFICITY

TYPES OF ENZYME SPECIFICITY when an enzyme can act and catalyze one unique reaction

ABSOLUTE SPECIFICITY

FACTORS THAT AFFECT BINDING OF ENZYME TO SUBSTRATE

ENERGY, MOLECULAR COMPATIBILITY, SPACE AVAILABILITY, SPECIFICITY

TYPES OF ENZYME SPECIFICITY when some enzymes act on different substrates belonging to the same group

GROUP SPECIFICITY

TYPES OF ENZYME SPECIFICITY an enzyme acts only on the specific isomer

STEREOISOMERIC

the enzyme changes in shape during binding to accommodate the substrate

INDUCED FIT MODEL

In this reaction, the entire enzyme is bound to substrate and a much higher rate of reaction is obtainedBecause the entire enzyme is present in the form of the complex, there is now no further increasein ES complex conc. No further increment in reaction rate ispossible

ZERO ORDER KINETIC

The rate observed reflects the low concentration of the ES complex

FIRST ORDER KINETIC

Optimum temperature considered favorable for enzyme activity

37-40

the point at w/c the reaction rate is greatest

OPTIMUM PH

Pepsin – active at _pH

1.5

ALP – active at_pH

10.5

ACTIVATORS

IRON, CALCIUM, ZINC, MAGNESIUM

Decrease the rate of enzyme reaction

INHIBITOR

Is not possible to remove the inhibitor

IRREVERSIBLE INHIBITION

COMPH Lesson 5

Jef Marc Valencia · 73問 · 2年前

COMPH Lesson 5