mid. 2 – Chemistry – Flashcards

Unlock all answers in this set

Unlock answers
question
Enzymes are the agents of _____
answer
metabolic function
question
Enzyme: a biological _____
answer
catalyst
question
Enzyme: a biological catalyst
with the exception of some____ that catalyze their own splicing (Section 10.4), all enzymes are_____
answer
RNAs. proteins
question
enzymes can ____ the rate of a reaction by a factor of up to _____ over an uncatalyzed reaction
answer
increase. 10 to the 20th
question
enzymes can ____  the rate of a reaction by a factor of up to ____ over an uncatalyzed reaction
answer
increase. 1020
question
some enzymes are so ____  that they catalyze the reaction of only one ____; others catalyze a family of similar reactions
answer
specific. stereoisomer
question
Enzymes produce products in very _____ -> often much greater than ____
answer
high yields. 95%
question

Enzymes can accelerate reactions as much as 1020 over uncatalyzed rates!

 

Urease is a good example:

Catalyzed rate: 3x104/sec

Uncatalyzed rate: 3x10 -10/sec

Ratio is:  !

answer
1 X 1014
question
 

D-amino acid oxidase only oxidizes ____ and not ____ .

answer
D-amino acids.  L-amino acids
question
[image]
answer
look at me again
question
[image]
answer
look at me again
question
 

The breakdown of glucose by ___  provides a prime example of a metabolic pathway. Ten enzymes mediate the reactions of glycolysis.

answer
glycolysis
question
 

Enzymes are highly regulated at

      the ___ level

      the ____ level

      the ____  level

answer

activity

protein

gene

question
 

Oxidoreductases

Act on many chemical groupings to add or remove ____  atoms or ______.

answer

hydrogen

electrons

question
Oxidoreductases
answer
Spell it
question
 

Transferases

Transfer functional groups between ___  and _____  molecules.

answer

donor

acceptor

question
Kinases are specialized ____  that regulate metabolism by transferring ______  from ATP to other molecules.
answer

transferases

phosphate

question
 

Transferases

answer
Spell it
question
 

Hydrolases

Add water across a _____ , hydrolyzing it.

answer
bond
question
Hydrolases
answer
Spell it
question
 

Lyases

Add ____,  _____ or _____ across double bonds, or remove these elements to produce double bonds or other cleavages involving electron rearragenement.

 

answer

water

ammonia

carbon dioxide

question
 

Lyases

 

answer
spell it
question
 

Lyases

Add water, ammonia or carbon dioxide across ____ , or remove these elements to produce ______or other cleavages involving _____ rearragenement.

 

answer

double bonds

double bonds

electron

question
 

Isomerases

Carry out many kinds of isomerization: ____ isomerizations, mutase reactions (shifts of chemical groups) and others.

answer
L to D
question

 

Isomerases

answer
Spell it
question
 

Isomerases

Carry out many kinds of isomerization: L to D isomerizations, ___ reactions (shifts of ____ ) and others.

answer

mutase

chemical groups

question
 

Ligases

Catalyze reactions in which two chemical groups are  ____ (or ligated) usually with the use of energy from ____.

answer

joined

ATP

question
 

Act on many chemical groupings to add or remove hydrogen atoms or electrons.

answer

Oxidoreductases

question

 

Transfer functional groups between donor and acceptor molecules.

answer
Transferases
question

Add water across a bond, hydrolyzing it.

answer

Hydrolases

question

 

Add water, ammonia or carbon dioxide across double bonds, or remove these elements to produce double bonds or other cleavages involving electron rearragenement.

answer
Lyases
question

 

Carry out many kinds of isomerization: L to D isomerizations, mutase reactions (shifts of chemical groups) and others.

answer
Isomerases
question

 

Catalyze reactions in which two chemical groups are joined (or ligated) usually with the use of energy from ATP.

answer
Ligases
question
 

Examples                  RXN

Oxidoreductasesà Alcohol Dehydrogenaseà turns ___ into ______.

answer

Ethanol

Acetaldehyde

question
 

Transferasesà Hexokinase à turns _____ into _____

 

answer

D-Glucose

D-Glucose-6-phosphate

question

Hydrolase à Carboxypeptidase à turns a molecule with a  _____ bond into a ____

 

answer

double

single

question

Lyases à Pyruvate decarboxylase à turns ___  into ____

 

 

answer

Pyruvate

Acetaldehyde

question
Isomerases à Maleate isomerase à Turns ___ into  ____

 

 

answer

Maleate

Fumarate

question

Ligases à Pyruvate Carboxylase à Turns  ___ into ____.

answer

Pyruvate

Oxaloacetate

question

  

_______à Alcohol Dehydrogenaseà turns Ethanol into Acetaldehyde

 

answer
Oxidoreductases
question

_______à Hexokinase à turns D-Glucose into D-Glucose-6-phosphate

 

answer
Transferases
question

 ______à Carboxypeptidase à turns a molecule with a double bond into a single

 

answer
Hydrolase
question

 ______à Pyruvate decarboxylase à turns Pyruvate into Acetaldehyde

 

answer
Lyases
question

 ______à Maleate isomerase à Turns Maleate into Fumarate

 

answer
Isomerases
question

 _______à Pyruvate Carboxylase à Turns Pyruvate into Oxaloacetate

answer
Ligases
question
 

ENZ.                 Optimum pH

 

Pepsin              _____

 

answer
1.5
question

                     pH 

Catalase      _____ 

 

answer
7.6
question

                 pH 

Trypsin     ______ 

 

answer
7.7
question

                           pH 

Fumarase         ____

 

answer
7.8
question

 

                                       pH

Ribonuclease               ____

Arginase                       ____

answer

7.8

9.7

question
 

______ changes the rate of the catalyze reaction ( rate ___ as temperature goes up)

 

 

answer

Temperature

increase

question
However, there is an optimum temperature, why?

 

• Increasing temperature will eventually lead to _______.

answer
protein denaturation
question

 

Enzyme Kinetics

answer
question
 Free Energy of RXN

For a reaction taking place at constant temperature and pressure, e.g., in the body→  _____.

 

                                 

answer
 A <=> B
question

the change in free energy is represented by this rxn

___________________

answer
ΔG°= ΔH° - TΔS°
question
 
 

The change in free energy is related to the equilibrium constant, Keq, for the reaction by

______________________________

 

answer
ΔG° = -RT in Keq
question
 

An enzyme alters the rate of a reaction, but not its _____ change or position of _______

answer

free energy

equilibrium

question
[image]
answer

look at me again

question
 

The rate of a reaction depends on its______ , D

answer
activation energy
question

 

The rate of a reaction depends on its activation energy, denoted as _____(or symbol is)?

answer
D
question
 

a enzyme provides an alternative pathway with a ____ activation energy

answer
lower
question
  left off on slide 16 on 06A enzymes I v 4.1 file
answer
question

Understand the difference between ΔG0 and ΔG0

 

 The overall free energy change, ΔG0, for a reaction is related

to the ________.

answer
equilibrium constant
question
The free energy of activation, ΔG0‡,  for a reaction is related to the _____.
answer
rate constant
question
 

The overall free energy change, _____  for a reaction is related

 

to the equilibrium constant

answer
ΔG0
question
 

The free energy of activation, ____ for a reaction is related

 

to the rate constant

answer
 ΔG0‡, 
question
[image]
answer
look at changes
question
 

         In an enzyme-catalyzed reaction  S → P

substrate, S: a ______

 active site: the small portion of the _______ where the substrate(s) becomes bound by ______ forces, e.g.,  ______bonding, _______attractions, van der Waals attractions

 

answer

reactant

enzyme surface

noncovalent

hydrogen

electrostatic

question
 enzyme-catalyzed reaction  S → P

Specificity is controlled by _____ - the unique fit of substrate with enzyme controls the selectivity for substrate and the product yield – all refered to as the  ______.

answer

structure

ACTIVE SITE

question
[image]
answer
question
 Two models have been developed to describe formation of the enzyme-substrate complex

 

lock-and-key model: substrate binds to that portion of the enzyme with a __________.

induced fit model: binding of the substrate induces a______ in the ______  of the enzyme that results in a complementary fit

answer

complementary shape

change

conformation

question
 

Two models have been developed to describe formation of the enzyme-substrate complex

_____: substrate binds to that portion of the enzyme with a complementary shape

______: binding of the substrate induces a change in the conformation of the enzyme that results in a complementary fit

answer

lock-and-key model

induced fit model

question
[image]
answer
question
[image]
answer
Formation of a prodcut
question

 For the reaction-->

A + B ---> P

The rate of reaction is given by rate equation--->

answer
Rate = k[A] f[B]g
question

Rate = k[A] f[B]g

 

Where k is a proportionality constant called the specific ________.

Order of reaction: the ______ of the exponents in the rate equation .

answer

rate constant

sum

question
File, Enzymes I 4.1. slide 24 ??
answer
question
[image]
answer
 

Chymotrypsin catalyzes the selective hydrolysis of peptide bonds where the carboxyl is contributed by Phe and Tyr

it also catalyzes hydrolysis of the ester bond of p-nitrophenyl esters

question
[image]
answer
question
 Non-Allosteric Enzyme Behavior

Chymotrypsin

 

Point at which the rate of reaction does ______, enzyme is _____ , maximum rate of reaction is _____.

 

answer

not change

saturated

reached

question
[image]
answer
question
 

Initial rate of an enzyme-catalyzed reaction versus substrate concentration...look at pic-->

 

answer
[image]
question
Michaelis-Menten Model

 

for an enzyme-catalyzed reaction--> (rxn)-->

 

answer
[image]
question
 

Michaelis-Menten Model

the rates of formation and breakdown of ES are given by these equations ---->

answer
[image]
question
 Michaelis-Menten Model

At the steady state the equation is-->

answer
[image]
question

 

Michaelis-Menten Model

when the steady state is reached, the concentration of free enzyme is the total less that bound in ES----represented by equation-->

 

answer

[E]=[E]t-[ES]

question

 

Michaelis-Menten Model

substituting for the concentration of free enzyme and collecting all rate constants in one term gives the equation--->

 

where KM is called the Michaelis constant

answer
[image]
question

KM is called the _____  _____.

answer
Michaelis constant
question
 Michaelis-Menten Model

in the initial stages, formation of product depends only on the rate of breakdown of ES---represented by equa.--->

answer
question

 Michaelis-Menten Model

if substrate concentration is so large that the enzyme is saturated with substrate [ES] = [E]T

equa.-->

answer
[image]
question
 Michaelis-Menten Model

substituting k2[E]T = Vmax into the top equation gives  --->

answer
[image]
question
 
when [S]= KM, the equation reduces to
answer
[image]
question
Graphical determination of Vmax and KM from a plot of reaction velocity, V, against substrate concentration, [S].
answer
[image]
question
 

Vmax is the constant rate reached when the enzyme is completely ______ with substrate, a value that frequently must be estimated from such a graph.

answer
saturated
question
 Lineweaver-Burk Plot

which has the form y = mx + b, and is the formula for a straight line . equation?

answer
[image]
question

 Lineweaver-Burk Plot

a plot of 1/V versus 1/[S] will give a ___ line with slope of KM/Vmax  and y intercept of 1/Vmax

such a plot is known as a Lineweaver-Burk ______  ______  ______.

answer

straight

double reciprocal plot

question

Lineweaver-Burk Plot

 

a plot of 1/V versus 1/[S] will give a straight line with slope of _______and y intercept of ______ such a plot is known as a Lineweaver-Burk double reciprocal plot

answer

KM/Vmax 

1/Vmax

question
 Lineweaver-Burk Plot

KM is the dissociation constant for ___ ; the greater the value of KM, the ____tightly S is bound to E

Vmax is the maximum ______

answer

ES

less

velocity

question
 Lineweaver-Burk Plot

_____ is the dissociation constant for ES; the greater the value of ____ , the less tightly S is bound to E

 ____ is the maximum velocity

answer

KM

KM

Vmax

question
 Lineweaver-Burk Plot

 

answer
[image]
question

Turnover Numbers

Vmax is related to the turnover number of _____:also called kcat

 

answer
enzyme
question

 Turnover Numbers

Vmax is related to the turnover number of enzyme:also called ______. 

 

answer
kcat
question

 Turnover Numbers

Vmax is related to the turnover number of enzyme:also called kcat

 

answer
[image]
question
 Turnover Numbers and KM

Values for some typical enzymes

answer
[image]
question
 Enzyme Inhibition

Reversible inhibitor: a substance that binds to an ____  to ____ it, but can be

answer

enzyme

inhibit

released

question

 Enzyme Inhibition

 

competitive inhibitor: binds to the ___ ____ site and blocks access to it by ____.

answer

active (catalytic)

substrate

question

 Enzyme Inhibition

 

noncompetitive inhibitor: binds to a site other than the _____ _______ ; inhibits the enzyme by changing its ___.

 

answer

active site

conformation

question
 Enzyme Inhibition

Irreversible inhibitor: a substance that causes inhibition that _____  _____ _____.

usually involves formation or breaking of  ___ ____ to or on the enzyme

answer

cannot be reversed

covalent bonds

question

 

__________: a substance that binds to an enzyme to inhibit it, but can be released

answer
Reversible inhibitor
question

 

__________: binds to the active (catalytic) site and blocks access to it by substrate

answer
competitive inhibitor
question

 

___________: binds to a site other than the active site; inhibits the enzyme by changing its conformation

answer
noncompetitive inhibitor
question
 

____________: a substance that causes inhibition that cannot be reversed

usually involves formation or breaking of covalent bonds to or on the enzyme

answer
Irreversible inhibitor
question
 Competitive Inhibition

substrate must compete with inhibitor for the _____; more substrate is required to reach a given ________.

answer

active site

reaction velocity

question
 Competitive Inhibition

substrate must compete with inhibitor for the active site; more substrate is required to reach a given reaction velocity

 

answer
[image]
question
 Competitive Inhibition

substrate must compete with inhibitor for the active site; more substrate is required to reach a given reaction velocity

we can write a dissociation constant, KI for EI

answer
[image]
question
look at me....
answer
[image]
question
Structures of succinate, the substrate of succinate dehydrogenase (SDH), and malonate, the competitive inhibitor. Fumarate (the product of SDH action on succinate) is also shown.  
answer
[image]
question

Competitive Inhibition

 

answer
[image]
question
Competitive Inhibition
answer
[image]
question
 Competitive Inhibition

 

 

In a Lineweaver-Burk double reciprocal plot of 1/V versus 1/[S], the  ______ (and the x intercept) changes but the y intercept does not _____.

 

answer

slope

change

question

 Competitive Inhibition

answer
[image]
question
 Noncompetitive Inhibition

 

 

several equilibria are involved.....

answer
[image]
question
 The maximum velocity VImax has the form
answer
[image]
question
Noncompetitivee inhibition
answer
[image]
question
 Noncompetitive Inhibition

 

because the inhibitor does not interfere with binding of substrate to the active site, KM is ______.

increasing substrate concentration cannot overcome ______  _______.

answer

unchanged

noncompetitive inhibition

question
Noncompetitive Inhibition
answer
[image]
question
Noncompetitive Inhibition
answer
[image]
question
Noncompetitive Inhibition
answer
[image]
question

 Inhibitor Type

Competitive Inhibitor

Specifically at the catalytic site, where it competes with ______ for binding in a dynamic equilibrium- like process. Inhibition is  ______ by substrate.

answer

 substrate

reversible

 

question

 Inhibitor Type

Competitive Inhibitor

Kinetic effect

 

Vmax is _______; Km, as defined by [S] required for 1/2 maximal activity, is increased.

answer
unchanged
question

 Inhibitor Type

Noncompetitive Inhibitor

 

Binds E or ES complex other than at the _____  site. Substrate binding ______, but ESI complex cannot form products. Inhibition ____ _____ reversed by substrate.

answer

catalytic

unaltered

cannot be

question

 Inhibitor Type

Noncompetitive Inhibitor

 

 

Km appears unaltered; Vmax is ________ proportionately to inhibitor _____________.

answer

decreased

concentration

question
 Other Types of Enzyme Inhibition

 

Uncompetitive- inhibitor _____ bind to the ES complex but not to free _____.   Vmax decreases and KM decreases.

 

 

Mixed- Similar to noncompetitively, but binding of I affects binding of S and vice versa.

 
answer

can

E

question
 Enzymes with Non-Michaelis Kinetics – Allosteric

Sigmoidal shape- characteristic of allosterism

Again Max. velocity reached, but different mechanism

answer
[image]
question
 What Factors Influence Enzymatic Activity

 

 

Enzymes are highly regulated at

the activity level

 

Substrate-level Control; Product inhibition

 

answer
question

What Factors Influence Enzymatic Activity

Rate slows as product ________.

 

Rate depends on ______  availability

 

________ effectors may be important

 

 

answer

accumulates

substrate

Allosteric

question

Feedback Control (inhibition)

 

 

The protein level

Enzymes can be modified _______: reversibly or irreversibly

Zymogens, isozymes and modulator proteins may play a role

 

answer
covalently
question

Translation – to make more or less ______.

Protein turnover

Compartmentalization

 

the gene level

Genetic controls - induction and repression

answer

 protein

 

question
[image]
answer
understand me
question
 Allosteric Enzymes

Allosteric: Greek allo + steric, other shape

Allosteric enzyme: an _____ whose biological activity is affected by other ______ binding to it.

these substances change the enzyme’s activity by altering the conformation(s) of its _____.

answer

oligomer

substances

4° structure

question
 Allosteric effector: a substance that modifies the behavior of an  _________; may be an

allosteric ______ or an allosteric _______.

answer

allosteric enzyme

inhibitor

activator

question
 Aspartate transcarbamoylase (ATCase)

   __________    _____________.

answer
feedback inhibition
question
[image]
answer
question
 ATCase

Figure à Rate of ATCase catalysis vs substrate conc.

answer
[image]
question
 ATCase

Figureà ATCase catalysis in presence of CTP; ATP

answer
[image]
question
 ATCase

catalytic unit:  ___ subunits organized into  trimers ___

regulatory unit: 6 subunits organized into 3 trimers

answer

6

3

question
 Allosteric Enzymes

The key to allosteric behavior is the existence of multiple forms for the ___ ___ of the enzyme.

answer
4° structure
question

 Allosteric Enzymes

 

allosteric effector: a substance that modifies the ____ of an allosteric enzyme

answer
4° structure
question

 Allosteric Enzymes

 

homotropic effects: allosteric interactions that occur when several ____ molecules are bound to the ____; e.g., the binding of ____  to _____

answer

identical

protein

aspartate

ATCase

question

  Allosteric Enzymes

 

heterotropic effects: allosteric interactions that occur when ______ substances are bound to the ______ ; e.g., inhibition of ATCase by ____  and activation by ______.

 

answer

different

protein

CTP

ATP

question
 Allosteric Enzymes

 

________: a substance that modifies the 4° structure of an allosteric enzyme

answer
allosteric effector
question
 Allosteric Enzymes

__________: allosteric interactions that occur when several identical molecules are bound to the protein; e.g., the binding of aspartate to ATCase

answer
homotropic effects
question

 Allosteric Enzymes

________: allosteric interactions that occur when different substances are bound to the protein; e.g., inhibition of ATCase by CTP and activation by ATP

 

answer
heterotropic effects
question
 General Features of Allosteric Regulation

Action at "another site"

Enzymes situated at key steps in ______ are modulated by

 

_______effectors.

answer

metabolic pathways

allosteric

question
 General Features of Allosteric Regulation

Action at "another site"

 

These effectors are usually produced _____ in the pathway

 

answer
elsewhere
question
 General Features of Allosteric Regulation

Action at "another site"

 

Effectors may be feed-forward ______ or feedback ____.

 

 

Kinetics are ____ ("S-shaped")

answer

activators

inhibitors

sigmoid

question
 {Sigmoid v (allosteric)} versus { [S] plot (non competitive inhibition) }. The dotted line represents the hyperbolic plot characteristic of normal Michaelis - Menten-type enzyme kinetics.
answer
[image]
question
 Models for Allosteric enzymes

The ______ Model

 

The _______ Model

answer

Concerted

Sequential

question
 The Concerted Model

Wyman, Monod, and Changeux - 1965

 

The enzyme has two conformations

R (relaxed): binds _____  tightly; the active form

answer
substrate
question
 The Concerted Model

T (tight or taut): binds _____ less tightly; the inactive form

answer
substrate
question
 The Concerted Model

 

In the absence of substrate, most enzyme molecules are in the  _______ form.

answer
T (inactive)
question

 The Concerted Model

 

The presence of ____ shifts the equilibrium from the T (inactive) form to the R (active) form

answer
substrate
question

 The Concerted Model

 

In changing from T to R and vice versa, all subunits change _________ simultaneously; all changes are concerted

answer
conformation
question
 The Concerted Model

Wyman, Monod, and Changeux - 1965

The enzyme has two conformations

________: binds substrate tightly; the active form

________: binds substrate less tightly; the inactive form

 

answer

R (relaxed)

T (tight or taut)

question
 Concerted Model

A ______ protein with two subunits

both change from ___ to ___ at the same time

answer

hypothetical

T

R

question
 Concerted Model

Figureà Monod-Wyman-Changeaux model

answer
[image]
question
[image]
answer
question
  Sequential Model

Koshland - 1966

the binding of substrate induces a conformational change from the ___ form to the ____ form

answer

T

R

question
 Sequential Model

Koshland - 1966

the change in conformation is induced by the fit of the  ______ to the enzyme, as per the induced-fit model of substrate binding

 

answer
substrate
question
 Sequential Model

Koshland - 1966

the change in conformation is induced by the fit of the substrate to the enzyme, as per the _____ of substrate binding

 

answer
induced-fit model
question
 Sequential Model

Figureà Sequential model for cooperative binding of substrate to an allosteric enzyme

answer
[image]
question

 Sequential Model

Figureà Allosteric activation and inhibition also occur by the induced-fit mechanism

answer
[image]
question
 Enzymes can be modified covalently

 

_______ Modification

_______ Modification

answer

Reversible

Irreversible

question
 Phosphorylation

the side chain -OH groups of Ser, Thr, and Tyr can form  _______ esters

phosphorylation by ATP can convert an inactive precursor into an ______ ______.

answer

phosphate

active enzyme

question
 

Irreversible Covalent Modifications:

Are known as ______

 

 

answer

Zymogens

question
 Zymogens

Zymogen: an _____ precursor of an ______; cleavage of one or more _____  ______ transforms it into the active enzyme

 

answer

inactive

enzyme

covalent bonds

question
 Zymogens

 Chymotrypsinogen

synthesized and stored in the _____

 a single polypeptide chain of 245 amino acid residues cross linked by five disulfide (-S-S-) bonds

answer
pancreas
question
 Zymogens

when secreted into the small intestine, the digestive enzyme ______ cleaves a 15 unit polypeptide from the N-terminal end to give p-chymotrypsin

answer
trypsin
question
 Zymogens

_________: an inactive precursor of an enzyme; cleavage of one or more covalent bonds transforms it into the active enzyme

answer
Zymogen
question
 The Active Site

1. Which amino acid residues on an enzyme are in the ____ _____  and  ____ the reaction?

answer

active site

catalyze

question
 The Active Site

2. What is the spatial relationship of the _______ ______ _______ residues in the active site?

answer
essential amino acids
question
 The Active Site

3. What is the _________ by which the essential amino acid residues catalyze the reaction?

 

answer
mechanism
question

 The Active Site

As a model, we consider chymotrypsin, an enzyme of the digestive system that catalyzes the selective hydrolysis of peptide bonds in which the carboxyl group is contributed by Phe or Tyr

 

answer
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

subtilisin, plasmin, TPA

Enzyme and substrate become linked in a ______ ______at

 

one or more points in the reaction pathway

answer
covalent bond
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

 

subtilisin, plasmin, TPA

The formation of the ________ ______provides chemistry that

 

speeds the reaction

answer
covalent bond
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

 

subtilisin, plasmin, TPA

All involve a _______ in catalysis - thus the name

 

answer
serine
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

subtilisin, plasmin, TPA

 

Ser is part of a "catalytic triad" of _____, _____, ______.

answer
Ser, His, Asp
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

subtilisin, plasmin, TPA

Serine proteases are _____ , but locations of the three

crucial residues differ somewhat

answer
homologous
question
 The Serine Proteases

Trypsin, chymotrypsin, elastase, thrombin,  

 

subtilisin, plasmin, TPA

Enzymologists agree, however, to number them always as His-

57, Asp-102, Ser-195

 

Burst kinetics yield a hint of how they work!

answer
question
 

Chymotrypsin

because Ser-195 and His-57 are required for activity, they must be close to each other in the active site

results of x-ray crystallography show the definite arrangement of amino acids at the active site

in addition to His-57 and Ser-195, Asp-102 is also involved in catalysis at the active site

answer
question
 Coenzymes

Coenzyme: _____ organic molecule that takes part in an _____ reaction and is regenerated for further reaction

 

 

answer

nonprotein

enzymatic

question
 Coenzymes

organic compounds, many of which are vitamins or are metabolically related to vitamins are ______ - molecules that bring unusual chemistry to the enzyme active site

 

answer
coenzymes
question
 Vitamins

Vitamins and coenzymes are classified as "___ ____" and "____ _____"

 

The water-soluble coenzymes exhibit the most interesting chemistry

 

answer

water-soluble

fat-soluble

question
 Vitamins

Fat-soluble Vitamins:_____,_____,_____,_____.

 

answer
A, D, E, K
question
 Vitamins

Water-soluble Vitamins:

  B1 – Thiamine  C – Ascorbic acid

  B2 -  Riboflavin 

  B3 -  Niacin

  B5 -  Pantothenic Acid

  B6 -  Pyridoxal

  B7 – Biotin

  B9 -  Folic acid

  B12 - Cyanocobalamin

answer
question
 Nicotinic Acid and the Nicotinamide Coenzymes

aka pyridine nucleotides

These coenzymes are _____ _____ ______

 

answer
two-electron carriers
question

Nicotinic Acid and the Nicotinamide Coenzymes

They transfer _____ ____ ____  to and from substrates

answer
hydride anion (H-)
question
 

Nicotinic Acid and the Nicotinamide Coenzymes

Two important coenzymes in this class:

 

Nicotinamide adenine dinucleotide ________

 

Nicotinamide adenine dinucleotide phosphate ______

 

answer

(NAD+)

(NADP+)

question
 NAD+/NADH

NAD+ is a ____ ____ oxidizing agent, and is reduced to ______.

answer

two-electron

NADH

question

 NAD+/NADH

NAD+ is involved in a variety of _____ ____ oxidation/reduction reactions.

answer
enzyme-catalyzed
Get an explanation on any task
Get unstuck with the help of our AI assistant in seconds
New