Zusammenfassung der Ressource
Enzymes I
- Properties
- Proteins
- Work @
physiological
conditions
Anmerkungen:
- Low temperature, neutral pH, atmospheric pressure, aqueous environment
- Efficient
- Active site
- Specific
Anmerkungen:
- A separate binding site determines the specificity of serine proteases.
- Chymotrypsin - large hydrophobic substrates
Trypsin - (+) substrates
Elastase - small substrates (glycine)
- Due to conformation
- Active site
- Where substrate binds
- Stereospecific
- Regulated
- Coenzymes
Anmerkungen:
- Non-protein parts of the enzymes
- Vitamins
Anmerkungen:
- Vitamins are precursors to coenzymes
- Thaimin (B1)
- Thiamine pyrophosphate
- Aldehyde transfer
- Covalent
intermediate
w/ keto
groups
- deficiency
- Beriberi
- Riboflavin (B2)
- Flavin Adenine
Dinucleotide (FAD)
- Redox
- Deficiency
- Cheliosis and angular
stomatitus, dermatitus
- Pyridoxine (B6)
- Pyridoxal Phosphate
- Group transfer
to/from AAs
- Covalent
complexes w/
amino groups
- Deficiency
- Depression,
confusion,
convulsion
- Nicotin acid (niacin)
- Nicotinamide adenine
dinucleotide (NAD+)
- Redox
- Deficiency
- Pellagra
- Used by alcohol
dehydrogenases to
abstract H from alcohols
- Classes
- Oxidoreducatases
- Oxidation-reduction
- lactate
dehydrogenase
- Transferases
- Group transfer
- NMP Kinase
- Hydrolases
- Hydrolysis Rxns
- Chymotrypsin
Anmerkungen:
- Mechanism of Chymotrypsin:
First, the subtrate binds.
- Next, histidine activates serine for nucleophilic attack.
- After that, the oxyanion tetrahedral intermediate is stabilized by H-bonds.
- Then, the cleavage of the peptide bond occurs.
- Serine protease
- Hydrolyzes peptide bonds
- Lyases
- Addition/removal
of groups to form
double bonds
- Fumarase
- Isomerases
- Isomerization
- Triose
phosphate
isomerase
- Ligases
- Ligation of two
substrates at the
expense of ATP
hydrolysis
- Aminoacyl-tRNA
synthetase
- Catalysis
- Orientation/proximity
- Induced fit model
- General acid/base catalysis
- Nucleophilic catalysis
- Stabilize transition state
- Metal ion catalyst