Day 9

Question 1

two categories of protein functions

Answer 1

catalytic and noncatalytic

Question 2

are most enzymes proteins or RNA molecuels

Answer 2

most are proteins, some are RNA molecules

Question 3

1+ inorganic ions, such as Fe, Mg, Mn, or Zn

Answer 3

cofactor

Question 4

complex organic or metalloorganic molecule that act as transient carriers of specific functional groups

Answer 4

coenzymes

Question 5

how are most coenzymes derived

Answer 5

from vitamins

Question 6

coenzyme or cofactor that is tightly bound

Answer 6

prosthetic group

Question 7

an enzyme with its bound coenzyme/cofactor

Answer 7

holoenzyme

Question 8

the protein only portion of a holoenzyme

Answer 8

apoenzyme or apoprotein

Question 9

enzyme class that transfers electrons

Answer 9

oxidoreductases

Question 10

enzyme class that does group transfer

Answer 10

transferase

Question 11

hydrolysis, what enzyme class

Answer 11

hydrolases

Question 12

cleaveage of C-C, C-O, C-N or other bonds by elimination, leaving double bonds or rings or addition of groups to double bonds

Answer 12

lyases

Question 13

transfer of groups within molecules to yield isomeric forms

Answer 13

isomerases

Question 14

formation of C-C, C-S, C_O, and C-N bonds by condensation reactions coupled to cleavage of ATP or similar cofactor

Answer 14

ligases

Question 15

movement of molecules or ions across membranes or their separation within membranes

Answer 15

translocases

Question 16

add phosphate groups to substrates or other enzymes

Answer 16

kinases

Question 17

provides a specific environment in which a given reaction can occur more rapidly

Answer 17

active site

Question 18

the molecule that is bound to the active site and acted upon by the enzyme

Answer 18

substrate

Question 19

starting point for either the forward or reverse reaction

Answer 19

ground state

Question 20

the point at which decay to substrate or product are equally likely

Answer 20

transition state

Question 21

how is activation energy lowered (3 ways)

Answer 21

binding energy, covalent bonding, enzyme function is impacted by binding specificity

Question 21

difference between the ground state energy level and the transition state energy level

Answer 21

activation energy

Question 22

how is binding energy used in lowering AE

Answer 22

energy taken from non covalent interactions between enzyme and substrate or receptor and ligand

Question 23

causes changes in the substrate and provides a lower energy, alternative pathway

Answer 23

covalent bonding

Question 24

two models of binding specifity

Answer 24

induced fit, lock and key

Question 25

types of catalysis

Answer 25

acid basis catalysis, covalent catalysis, metal ion catalysis

Question 26

protons transferred between E and S or intermediate

Answer 26

acid base catalysis

Question 27

uses H+ and OH- ions in water

Answer 27

acid base catalysis

Question 28

transient covalent bond forms between E and S

Answer 28

covalent catalysis

Question 29

help with orientation, stabilize charge, mediate red-ox rxns, can be bound to E or free

Answer 29

metal ion catalysis

Question 30

determining the rate of a rxn and how it changes in response to changes in experimental parameters

Answer 30

enzyme kinetics

Question 31

initial transient pd during which ES builds up; VERY brief, often too short to be observed

Answer 31

pre steady state

Question 32

period during which [ES] and other intermediates remain constant

Answer 32

steady state

Question 33

the traditional analysis of reaction rates

Answer 33

steady state kinetics

Question 34

what remains constant in our assumptions

Answer 34

ES and S concentrations

Question 35

what is greater than what in our assumptions

Answer 35

[S]&raquo_space;» [E]