BCH210H1 Lecture Notes - Lecture 18: Isomerase, Alcohol Dehydrogenase, Glucosidases

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Reinhart Reithmeier

Document Summary

Catalysed reactions proceed at extraordinarily fast rates. Living systems use enzymes to accelerate & control rates of biochemical reactions. Highly specific for their substrates: often- stereospecificity (usually l-isomers b/c common in living organisms) Specificity almost 100: very little/no waste product. Almost all enzymes are proteins: ex. ribosomes made from rna, not all enzymes are proteins, not all proteins are enzymes. If coenzymes exist, they are required for enzyme"s full activity: oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase. Characteristics: use coenzyme (nad+, fad+, tale-tell signs of oxidoreductase, one substrate oxidized, other substrate reduced, oxidized loses electron, reduced gains electron. Lactate dehydrogenase: substrate: l-lactate, product: pyruvate + nadh + h+ Alanine transaminase: uses co-subsrate alpha-ketogluterate to transfer amine group, produces l-glutamate. Carnitine acyltransferase: substrate: fatty acyl coa, enzyme: transfer acyl group to l-carnitine, products: acylcarnitine & coa. Function: break bonds with h2o as substrate: uses hydrolytic reaction to break bonds. Pyrophosphatase: substrate: pyrophosphate, enzyme: pyrophosphate, product: phosphate.