chapter 16 - metabolism Flashcards
metabolism
refers to chemical processes within a cell or organism
starts with digestion
nutrients
biomolecules which provide energy
(proteins, triglycerides, carbohydrates, minerals, vitamins, water)
macronutrients/ micronutrients
hydrolysis of carbohydrates
amylase in saliva
- starch molecules - disaccharides in mouth (maltose)
- disaccharides - monosaccharides in small intestine (glucose)
require 2 different enzymes
hydrolysis of proteins
pepsin (stomach) commences process
protease is general term
- protein - polypeptides in stomach
- polypeptides - dipeptides in small intestine
- dipeptides - amino acids in intestines
hydrolysis of triglycerides
catalysed by lipase
triglycerides - diglycerides + fatty acid - monoglycerides + 2 fatty acids - glycerol + 3 fatty acids
in small intestine
hydrolysis of cellulose
cellulase
- human do not have cellulase
- pass as dietary fibre
- small amount can be hydrolysed by bacteria in gut
- cows have sufficient bacteria to synthesise cellulase
enzymes
- proteins that act as biological catalysts
- only act in narrow pH and temp ranges
tertiary structure - active site
- substrate
- bind through intermolecular forces
lock and key model
active site fits substrate perfectly, forming enzyme - substrate complex
optical isomer and enzymes
- amino acids are chiral
- only one enantiomer of each amino acid is used to build proteins
- enzymes must distinguish between enantiomers, by being chiral
- only one enantiomer will fit in active site
- intermolecular forces are formed between substrate and groups on enzyme surface (all - except covalent)
- weaken peptide link and make it easier to break
induced fit
slightly flexible active site (mold around substrate)
coenzymes
- many can’t function without cofactor
- metal ion or non-protein organic compound (coenzyme)
change shape of enzyme, changing binding properties of active site, allowing substrate to bind
enzyme activity
rate of reaction
substrate turned into product per unit of time
enzymes and pH
operate best at optimum pH
denature
TS depends on bonds between side chains
ionic bonds between NH3+ and COO- in side chains
pH change can cause NH3+ to lose an H+ and COO- to gain an H+, removing the ionic bond
Arg + Lys positive
Asp + Glu negative
enzymes and temp
operate best at optimum temp (37˚C)
intermolecular bonds broken
denatured
coagulation
after denaturation
proteins clump together again but working shape is lost