STRUCTURE OF ENZYMES
PRESENTEDBY :
….
VIVEKANAND COLLEGE KOLHAPUR
INTRODUCTION :
• ENZYMES:
• ENZYMES ARE BIOLOGICAL CATALYSTS.
• ENZYMES SPEED UP THE RATE OF THE BIOCHEMICAL REACTION.
• MOST ENZYMES ARE THREE DIMENSIONAL GLOBULAR PROTEINS
(TERTIARY AND QUATERNARY STRUCTURE).
• RNA SPECIES ACT AS ENZYMES ARE CALLED AS RIBOZYMES.
STRUCTURE OF ENZYMES:
• ENZYMES ARE MADE UP OF APOENZYME (PROTEIN) AND COENZYME
(NON-PROTEIN)
• COENZYME:
• NON PROTEIN ORGANIC COMPONENT.
• LOOSELY BOUND TO THE APOENZYME.
• ACTS AS A DONOR OR ACCEPTOR OF GROUP OF ATOM.
• EX. NAD ,FAD.
COFACTOR:
• NON PROTEIN INORGANIC COMPONENT.
• MAY BE TIGHTLY BOUND OR LOOSELY BOUND.
• BRINGING GROUP TO BIND ENZYMES AND SUBSTRATE.
• EX. METAL IONS LIKE CU+2,ZN+2,MG2+.
• NON PROTEIN COMPONENT FIRMLY ATTACHED TO PROTEIN.
• ORGANIC OR INORGANIC.
• EITHER COENZYME OR COFACTOR.
• REQUIRED FOR EFFECTIVE CATALYSIS.
• BIOCYTIN,FE AND CU, MO AND FE ETC.
PROSTHETIC GROUP :
ACTIVE SITE OF ENZYMES:
ACTIVE SITE
BINDING SITE CATALYTIC SITE
IT CHOOSES THE SUBSTRATE
AND BINDS IT TO ACTIVE SITE.
IT PERFORMS THE CATALYTIC
ACTION OF ENZYME.
SUBSTRATE:
• THE REACTANT IN BIOCHEMICAL REACTION IS TERMED AS
SUBSTRATE.
• WHEN A SUBSTRATE BINDS TO AN ENZYME IT FORMS AN ENZYME
SUBSTRATE COMPLEX.
SUBSTRATE JOINS ENZYME
FACTORS AFFECTINGRATE OF ENZYME CATALYSED
REACTIONS:
• TEMPERATURE
• HYDROGEN ION CONCENTRATION
EFFECT OF TEMPERATURE:
• RAISING THE TEMPERATURE INCREASES THE RATE OF ENZYME
CATALYZED REACTION BY INCREASING KINETIC ENERGY OF REACTING
MOLECULES .
• ENZYMES WORKS MAXIMUM OVER A PARTICULAR TEMPERATURE
KNOWN AS OPTIMUM TEMPERATURE.
• HOWEVER SOMETIMES HEAT ENERGY CAN ALSO INCREASE KINETIC
ENERGY TO A POINT THAT EXCEED THE ENERGY BARRIER WHICH
RESULTS IN DENATURING OF ENZYMES.
EFFECT OF PH:
• RATE OF ALMOST ALL ENZYMES CATALYZED REACTIONS DEPENDS ON
PH.
• MOST ENZYMES EXHIBIT OPTIMAL ACTIVITY AT PH VALUE BETWEEN 5
AND 9.
• HIGH OR LOW PH VALUE THAN OPTIMUM VALUE CAUSE IONIZATION
OF ENZYME WHICH RESULTS IN DENATURATION OF ENZYME .
structure of enzyme.PDF

structure of enzyme.PDF

  • 1.
    STRUCTURE OF ENZYMES PRESENTEDBY: …. VIVEKANAND COLLEGE KOLHAPUR
  • 2.
    INTRODUCTION : • ENZYMES: •ENZYMES ARE BIOLOGICAL CATALYSTS. • ENZYMES SPEED UP THE RATE OF THE BIOCHEMICAL REACTION. • MOST ENZYMES ARE THREE DIMENSIONAL GLOBULAR PROTEINS (TERTIARY AND QUATERNARY STRUCTURE). • RNA SPECIES ACT AS ENZYMES ARE CALLED AS RIBOZYMES.
  • 3.
    STRUCTURE OF ENZYMES: •ENZYMES ARE MADE UP OF APOENZYME (PROTEIN) AND COENZYME (NON-PROTEIN) • COENZYME: • NON PROTEIN ORGANIC COMPONENT. • LOOSELY BOUND TO THE APOENZYME. • ACTS AS A DONOR OR ACCEPTOR OF GROUP OF ATOM. • EX. NAD ,FAD.
  • 4.
    COFACTOR: • NON PROTEININORGANIC COMPONENT. • MAY BE TIGHTLY BOUND OR LOOSELY BOUND. • BRINGING GROUP TO BIND ENZYMES AND SUBSTRATE. • EX. METAL IONS LIKE CU+2,ZN+2,MG2+.
  • 5.
    • NON PROTEINCOMPONENT FIRMLY ATTACHED TO PROTEIN. • ORGANIC OR INORGANIC. • EITHER COENZYME OR COFACTOR. • REQUIRED FOR EFFECTIVE CATALYSIS. • BIOCYTIN,FE AND CU, MO AND FE ETC. PROSTHETIC GROUP :
  • 6.
    ACTIVE SITE OFENZYMES: ACTIVE SITE BINDING SITE CATALYTIC SITE IT CHOOSES THE SUBSTRATE AND BINDS IT TO ACTIVE SITE. IT PERFORMS THE CATALYTIC ACTION OF ENZYME.
  • 7.
    SUBSTRATE: • THE REACTANTIN BIOCHEMICAL REACTION IS TERMED AS SUBSTRATE. • WHEN A SUBSTRATE BINDS TO AN ENZYME IT FORMS AN ENZYME SUBSTRATE COMPLEX. SUBSTRATE JOINS ENZYME
  • 8.
    FACTORS AFFECTINGRATE OFENZYME CATALYSED REACTIONS: • TEMPERATURE • HYDROGEN ION CONCENTRATION
  • 9.
    EFFECT OF TEMPERATURE: •RAISING THE TEMPERATURE INCREASES THE RATE OF ENZYME CATALYZED REACTION BY INCREASING KINETIC ENERGY OF REACTING MOLECULES . • ENZYMES WORKS MAXIMUM OVER A PARTICULAR TEMPERATURE KNOWN AS OPTIMUM TEMPERATURE. • HOWEVER SOMETIMES HEAT ENERGY CAN ALSO INCREASE KINETIC ENERGY TO A POINT THAT EXCEED THE ENERGY BARRIER WHICH RESULTS IN DENATURING OF ENZYMES.
  • 11.
    EFFECT OF PH: •RATE OF ALMOST ALL ENZYMES CATALYZED REACTIONS DEPENDS ON PH. • MOST ENZYMES EXHIBIT OPTIMAL ACTIVITY AT PH VALUE BETWEEN 5 AND 9. • HIGH OR LOW PH VALUE THAN OPTIMUM VALUE CAUSE IONIZATION OF ENZYME WHICH RESULTS IN DENATURATION OF ENZYME .