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20 Cards in this Set

  • Front
  • Back

PKA's for Asparate, Gltuatmate, Histidine, Cystine, Tyrosine, Lysine, Arginine

Name 6 major enzyme classifications and what they do

oxidoreductases - Redox reaction


transferases - Move group


hydrolases - Cut with water


lyases - Cut without using H2O or redox


isomerases - Isomerize


ligases - Combine

How does enzyme act as catalyst

Stabalizing normal transition state or providing different pathway

Ways that transition states stabalize transitions states:

Induced Fit


Acid Base catalysis


Covalent Catalysis


Metal Ion catalysis

Cofactors of:


Activation transfer


vs


Redox

Activation transfer use the transfering group as cofactor


Redox transfers electrons and does not from covalent bonds



Describe mechanism for serine Proteases



Stabilizes intermediate through H bonding and covalent bonding.


Holds Reactants where they need to be in order to be "attached"

Explain Michaelis-Menton Equation Kinetics

Vi=(Vmax [S])/[Km+S]


Initial speed = how fast it is 50% saturated


Km= substrate affinity higher is greater affinity *also the substrate concentration needed to reach 1/2 Vmax


Vmax= Max velocity at infinite concentration - Reaction won't go any faster

Compare Glucokinase vs Hexokinase with respect to their Km's

Hexo: Low Km = fast uptake


Gluco: Higher= slower uptake

How does Km and Vmax change with Comp vs noncomp inhibitors

Competetive:


Km higher Vmax the same


Non Comp:


Km SAME Vmax lower

How does enzyme concentration change with rates of transcription or degradation?

More transcription= more enzymes

More degradation = less enzymes


Alosterism and activation vs inhibition

Activation binds to keep it relaxed


Inhibition binds to keep it tense

R vs T in enzyme bindong

R=Relaxed and able to do work


T= Tense and not able to work

Protenolysis

Changing of Zymogens to heir active state by removing part of the protien

Reversale Phosphorilization

Adding or removing a Phosphorylate group to activate to deactivate a protein



How does substrate concentration affect Vi?

Higher S, higher Vi. Vmax times S and Km PLUS S

Thiamins phosporilase

Cofactor



Biotin

Water soluble B-Vitamin used as coenzyme

Pyrodoxal Phospate

Coenzyme that reacts with amine group of amino acid

Covalent Modificaitons

Phyosphoralization of Serine, Tyrosine and sometimes threonine


Changes activity of protein


Can be dephosphoralized and return to previous state.

Protien protien interactions

When one protein interacts with another protein. GPCR for Ex.