Chem ch 19 Flashcards
active site is the part of enzyme with…(active in SC)
a specific shape and specific chemical make up.
substrate is…
a reactant in an enzyme-catalyzed reaction
Specificity of the enzyme is the…(the enzyme must be specific to S or R)
limitation of the activity of an enzyme to a specific substrate, specific reaction, or specific type of reaction
specificity
limitation of the activity of an enyzme to specific substrate or specific reaction
turnover number
10 - 10,000,000 molecules per second. The maximum number of substrates at which an enzyme can act upon per unit of time. ex - catalase is 10 (7)/ per second - very fast
cofactor and co-enzyme
non-protein part of an enzyme that is essential for the activity of the enzyme
cofactors are made of what?
minerals (metal ions)
co-enzyme is the…(it’s not the co-factor)
organic molecule (vitamins)
trace minerals (FFCK MZ)
are co-factors - CU2+, Fe2+, Fe3+, K+, Mg2+, Zn2+. They do coordinate covalent bond - covalent that is formed by sharing electrons, but one part is providing 2 electrons. the other is accepting. The act as Lewis acid, accepting electrons.
enzyme nomenclature
2 parts: identify the substrate that which the enzyme is acting upon. Describe the reaction. Family ending - ase. ie - pyruvate carboxylase
oxidase
adding oxygen
reductase
removing O2
dehydrogenase
adding or removing H
types of transferase (kin and tran can transfer)
A) kinase
B) transaminase
hydrolase (PLLAN your watering)
enzymes that catalyze the cleavage of a covalent bond using water
A) lipase B) protease C) amylase - sugar D) nulcease - DNA or RNA E) ligases
isomerase
converting one isomer to another one
lyase (lays is basic math)
adding or removing functional group using something other than water
decarboxylase
removing COO- and (CO2)
deaminase
remove amino group
dehydrotase
removing H2O
hydrotase
adding H2O
ligases (ligase is the ligament to hold SoCal together)
linking or bonding 2 substrates together: A) sythetase (using ATP - form product by adding 2 substrates) B) carboxylase
models that describe how enzymes work
lock and key and induced fit model
lock and key
when substrate fits into active site of the enzyme as a key fits into a lock
induced fit model
active site of the enzyme is flexible and it changes it’s shape to fit the substrate
abilities of enzymes (ability of enzyme to COPE)
1) proximity effect
2) orientation effect
3) catalytic effect
4) energy effect
proximity effect
enzymes are able to position on the substrate at the active site and bound to the substrate. ex - induced fit model
orientation effect
enzyme is holding the substrate at the exact distance and exact orientation
factors that effect enzyme activity (PETS even effect enzyme activity)
1) substrate concentration
2) enzyme concentration
3) temperature effect
4) pH change effect
substrate concentration - what is it? (can’t have substrate without rate)
concentration of substrate X is rate of biochemical reaction until all of the active sites are fully occupied (enzyme is saturated)
enzyme concentration
rate of the biochemical reaction is directly proportional to the enzyme concentration
temperature effect (at what temp?)
most enzymes denature and they lose the activity about 50 - 60 degrees C. high temp is killing the enzyme
pH effect
moste enzymes have optimum point at normal and/or buffered pH of the environment. most at pH 5 to 9.
activation energy (activate the intermediate!)
the difference in energy in between the intermediate and the reactant
catalysts do what?
just lower activation energy point
substrate is really just the…
reactant
R + E —- SE — PE – P + E
reaction plus enzyme = product, but the enzyme is still attached to product. it is released later
important co-enzymes (B a FAN of co-enzymes)
co-enzyme A, B12, FAD, NAD+
oxidoreductase
catalyze oxidation-reduction reactions of substrate molecules, most commonly addition or removal of oxygen or hydrogen.
when looking at substrate and reactant (if it’s on the test) and she asks what reaction, if its the same molecule with different connectivity, it’s…
isomerization
kinase (think of physio)
transferring phosphate group
transaminase
transferring amino group
types of lyase (the lyase-on hides the problems - HDDD)
A) decarboxylase
B) deaminase
C) dehydrotase
D) hydrotase
