Enzymes, Part 1 Flashcards Preview

Vet Prep: Cell Bio & Homeostasis > Enzymes, Part 1 > Flashcards

Flashcards in Enzymes, Part 1 Deck (27)
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1
Q

enzymes

A
  • act as mediators for all reactions in biological systems
  • are substrate-specific protein catalysts
  • they increase the rate of reactions without being changed or used up during process
  • selectively channel reactants (called substrates) into energetically favorable pathways
  • 3D structures of proteins generates sites for other molecules allowing reversible binding of them
2
Q

oxidoreductases

A
  • catalyze reactions in which one molecule is oxidized while the other is reduced, transfer of electrons H+ (oxidases, reductases, dehydrogenases)
  • ex: lactate – lactate dehydrogenase – pyruvate
3
Q

transferase

A
  • transfer carbon, nitrogen or phosphate containing groups

- ex: serine – serine hydroxymethyl transferase – glycine

4
Q

hydrolases

A
  • enzymes that catalyze a hydrolytic cleavage reaction (=t transfer or functional groups to water) (nucleases and proteases)
  • catalyze cleavage of bonds by addition of water
  • ex: urea – urease – carbone dioxide and ammonia
5
Q

lyases

A
  • catalyze the cleavage of C-C, C-S, and C-N bonds, addition of groups to double bonds or formation of double bonds by removal of groups
  • ex: pyruvate – pyruvate decarboxylase – acetaldehyde + carbon dioxide
6
Q

isomerases

A
  • catalyze the rearrangement of bonds within a single molecule, transfer or groups within molecules to yield isomeric forms
  • catalyze racemization of optical or geometric isomers
  • ex: methylmalonyl CoA – methylmalonyl CoA mutase – succinyl CoA
7
Q

ligases

A
  • join together (ligate) two molecules in an energy-dependent process (DNA ligase joins 2 DNA molecules), formation of C-C, C-S, C-O and C-N bonds by condensation actions coupled to cleavage of ATP or similar cofactor
  • catalyze formation of bonds btwn carbon and O,S,N coupled to hydrolysis of high-energy phosphates
  • ex: pyruvate – pyruvate carboxylase – oxaloacetate
8
Q

polymerases

A
  • catalyze polymerization reactions such as synthesis of DNA and RNA
9
Q

proteases

A
  • break down proteins by hydrolyzing bonds btwn amino acids
10
Q

kinases

A
  • catalyze the addition of phosphate groups to molecules
11
Q

ATPases

A
  • hydrolyze ATP (Na, K ATPase)
12
Q

synthases

A
  • synthesize molecules in anabolic reactions by condensing 2 smaller molecules together (ATP synthase)
13
Q

phosphatase

A
  • catalyze hydrolytic removal of a phosphate group from a molecule
14
Q

synthetase vs synthase

A

synthetase requires ATP, synthase does not require ATP

15
Q

phophatase vs phosphorylase

A

phosphatase uses water to remove phosphoryl group, phosphorylase uses Pi to break a bond and generate a phosphorylated product

16
Q

dehydrogenase

A
  • NAD+/FAD is an electron acceptor in a redox reaction
17
Q

oxidase vs oxygenase

A

oxidase: O2 is the acceptor and oxygen atoms are not incorporated into substrate
oxygenase: one or both oxygen atoms are incorporated

18
Q

active sites

A
  • special pocket on enzymes that have high specificity
  • contains AA side chains that participate in substrate binding and catalysis
  • this binding causes a conformational change in the enzyme that allows catalysis (EP)
19
Q

cofactors

A
  • metal ions such as Cu2+ and Fe2+
20
Q

holoenzyme

A

active enzyme E + CF (enzyme + cofactor)

21
Q

apoenzyme

A

inactive enzyme E - CF (enzyme - cofactor)

22
Q

coenzyme

A
  • nonprotein small organic molecule

- many are derived from vitamins

23
Q

cosubstrates

A
  • transiently associated
24
Q

prosthetic groups

A
  • permanently bound
25
Q

regulation

A
  • enzyme activity can be regulated (increased or decreased) so that the rate of product responds to cellular needs
26
Q

location in cell

A
  • many enzymes are located in specific organelles in cell (compartmentalization) -> some reactions are isolated from others (avoiding competition for substrate or enabling more favorable conditions)
27
Q

stabilizing the transition state

A
  • an enzyme can greatly increase the concentration of the reactive intermediate that can be converted to product accelerating the reaction