MCB Lec 9

the study of reaction rates that are catalyzed by a purified enzyme

milder reaction constants, faster reaction rates, more specific entry point, sometimes need a cofactor

class of enzyme A-+ B to A+B-, oxio reductions , dehdroginase and the O2 acceptor

A-B + Cto A+ B-C, enzymes transferrinf group from donor to acceptor

A-B + H2O to A-B B-OH, catalyse the hydrolisi of various bonds

A-B to A+B + X-Y, cleaves C-C C-N C-O bonds with hydrolysis or oxidation , molecule is elimentaed and forms a new double bond

A-B to A-B,catalyzes changes within 1 molecule

A+ B to A-B, catalyzes the joining of two molecules with accomanying hydrolsis of diphosphate bond in ATP or similar triphosphate

an additional chemical componenet other than amino acid residues that is required for the activity of some enzymes

cofactor that is a complex organic molecule

a coenzyme that is tightly or even covalently bond to the enzyme protien

a compllete calatillically active enzyme together bound with its coenzyme and/or metal ions

the protien part of the holoenzyme

substrate matches perfectly to enzyme site

once the substrate binds the enzyme around it molds to fit.

a proton is transferred between the enzyme and substrate

a covalent bond forms between the enzyme and substrate

Relevant when a reaction involves more than one substrate via favorable orientations

Metal ion can function and facilitate the formation of the nucleophile or serve as an electrophile

enzyme donates a proton to the substrate

enzyme abstracts a proton from the substrate

1. binds to substrate
2. positiong places the substrate behinf the lysozome residues
3. Activation ASP 52 acts as a nucleophile and forms a temp bond with sugar
4. Involvement of water GLu 35 is negative and water joins sugar H+ joins Glu35
5. Hydrolysis the subar bond is hydrolisized and split