Enzyme pt. 2 (Quiz 1) Flashcards

(50 cards)

1
Q

Enzymes are classified according to the ___?

A

type of reaction they catalyze

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Classification of Enzymes

  • EC First Integer: ____ of enzyme catalyzed reactions
  • 2nd integer: a ___
  • 3rd number: ___ depending on 1st and 2nd integer
  • 4th number: ____
A

Classification of Enzymes
* six major classes
* a subclass
* subclassification
* serial number

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

_______

rate of a reaction between ____ molecules is ____ if they are abstracted from ____ and held in ____ proximity to each other (in the enzyme’s active site)

A

Facilitation of Proximity
* two
* enhanced
* dilute solution
* close

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

to increase the effective concentration of the reactants

A

Propinquity effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

In Covalent catalysis – amino acid side chains :

A

nucleophilic groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

This mechanism involves the transient covalent binding of the substrate to an amino acid residue in the active site. Generally, this is to the hydroxyl group of a serine, although the side chains of threonine, cysteine, histidine, arginine and lysine can also be involved.

A

covalent catalysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Modes of Enhancement of Rates of Bond Cleavage / Catalytic Mechanisms (6)

A
  • Facilitation of Proximity
  • Covalent Catalysis
  • General Acid-Base Catalysis
  • Binding Energy Catalysis
  • Metal-ion Catalysis
  • Molecular Distortion and Shape Change
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

this would determine the ionization state of an amino acid side chain

A

pH of the active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

For acid-base catalysis, _____ is the most versatile amino acid due to its pk, which means that in most physiological situations it can act as either a proton donor or proton acceptor.

A

histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

refers to weak acids

A

proton donors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

refers to weak bases

A

proton acceptors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

______

  • The preceding ____ groups can potentially serve as either proton donors or proton acceptors.
  • This is ____ on many factors including the ____ nature of the substrate, any ____ involved, and the ___ of the active site
  • Generally,these ____ will interact together with the ____, or in conjunction with water or other weak, organic acids and bases found in cells.
A
  • acid-base catalysis
  • functional
  • dependent, molecular, co-factors, pH
  • amino acids, substrate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

_____

  • is involved in a majority of ____ reactions . it needs to be distinguished from ____ acid-base catalysis.
  • the _____ aids in stabilizing the transition state via ____ of a proton.
  • Therefore, the rate of the _____ is dependent on the _____ as well as the appropriate ____ state.
A

General Acid-Base Catalysis
* enzymatic
* specific
* buffer
* donation or removal
* reaction
* buffer concentration
* protonation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

catalytic factors in the binding of a substrate and enzyme:

1) transient____ of substrate and enzyme ____ by reducing the ______ of the two molecules,
2) solvation ____ of the _____ thermodynamically favorable, and
3) substrate and enzyme _____ changes.

A
  • limiting
  • movement
  • relative motion (or entropy)
  • distruption
  • water shell
  • conformational
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

accounts for the overall lowering of activation energy for a reaction, and it can also be considered as a catalytic mechanism for a reaction.

A

binding energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

_______

  • Various metals, all ____ charged and including zinc, iron, magnesium, manganese and copper, are known to form ____ with different enzymes or substrates.
  • This ____ complex can aid in the _____ of the substrate in the ______, and
  • metals are known to mediate _____ reactions by ____ changes in their ____ states (like Fe³+ to Fe2+).
A

Metal lon Catalysis

  • positively
  • complexes
  • metal-substrate-enzyme
  • orientation
  • active site
  • oxidation-reduction
  • reversible
  • oxidation
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Clinical Use of an Enzyme pt.2

  • Enzyme activity can be ____ genetically
  • A _____ in an enzyme can alter its ____ affinity, co-factor ____ stability etc. which can be used as a _____ in comparison with ____ enzyme
  • Loss of _____ presence due to genetic mutation as detected by ____ enzyme substrate and/or lack of ____ leading to a _____
  • NOTE: _____ that identify specific messenger RNA or DNA sequences are replacing many ____ enzymatic based markers of genetic disease
A
  • altered genetically
  • mutation
  • substrate
  • binding
  • diagnostic
  • normal
  • enzyme
  • increased
  • product
  • dysfunction
  • PCR techniques
  • traditional
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Clinical Use of Enzyme pt. 1

  • Enzyme Activity in Body Fluids Reflects ____ Status
  • Enzyme Activity Reflects the Presence of ____ or _____
  • Activity of serum enzymes _____ in presence of an _____
    (ex. some insecticides inhibit serum cholinesterases)
  • Determine co-factor ____(like an essential vitamin) by ____
    (ex. add back vitamin to assay, if activity increases, suggests deficiency in that vitamin)
A
  • Organ
  • Inhibitors or Activators
  • decreases
  • inhibitor
  • deficiencies
  • enzyme activity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

An ____ is a blood test or urine test that measures levels of certain enzymes to assess how well the body’s systems are functioning and whether there has been any tissue damage.

A

enzyme test

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Common Enzymes used for clinical diagnosis

A
  • alanine aminotransferase (ALT, also called glutamate pyruvate transaminase, GPT)
  • alkaline phosphatase
  • amylase
  • aspartate aminotransferase
  • creatine kinase
  • lactate dehydrogenase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

evaluate liver function and diagnose liver diseases such as hepatitis and cirrhosis.

A

alanine aminotransferase

22
Q

assess liver and bone disorders. when levels are elevated it can indicate cholestasis (bile flow obstruction), liver disease, or bone diseases such as Paget’s disease

A

alkaline phosphatase

23
Q

diagnose acute pancreatitis, and other conditions like salivary gland infections or intestinal obstruction

24
Q

assess liver function. Elevated levels can indicate liver damage but can also be associated with heart or muscle injury

A

aspartate aminotransferase

25
diagnose **muscle damage**, including conditions like **myocardial infarction** (heart attack) and **rhabdomyolysis**
creatine kinase
26
diagnosis of various conditions, including ***hemolysis*, liver disease, and certain cancers** (tissue damage)
lactate dehydrogenase
27
Chemical reaction need an initial input of energy
THE ACTIVATION ENERGY
28
During this part (activation energy) the reaction of the molecules are said to be in a ?
Transition state
29
**Enzyme makes the reactions go faster by...** * Increasing the ____ make **molecules move faster** * _____ systems are **very sensitive** to _____ changes. * Enzymes can increase the _____ of reaction without increasing/requiring an increase in the ______ * They do this by **lowering** the _ energy. * They **create a new reaction pathway** "a ____"
* temperature * Biological, temperature * rate of reactions, temperature. * activation energy. * "a short cut"
30
**Enzyme Specificity** * Enzymes have varying degrees of ____for substrates * Enzymes may recognize and catalyze: o a ___ substrate o a ___ substrate o a **particular type** of bond
* specificity o **single** o **group of similar**
31
**Lock-and-Key Model** In the lock-and-key model of enzyme action: * The **active site** has a ___ shape. * Only substrates with the ____ shape can fit. * The ____ is a key that fits the lock of the ___ .
* **rigid** shape. * **matching** shape * substrate, * active site
32
**The Lock and Key Hypothesis** * **Temporary** structure called the _____ complex **formed** * **Products** have a different ____ from the substrate * **Once formed,** they are ____ from the ____ * **Leaving** it ___ to become **attached** to another ____ * This *explains enzyme specificity* * This *explains the loss of activity* when enzymes denature
* enzyme-substrate * shape * released, active site * free, substrate
33
**Enzyme changes shape with substrate** people-pleaser na enzyme
Induced Fit Theory
34
The **induced-fit model** of enzyme action: * The **active site is ____, not rigid**. * The **shapes** of the enzyme, active site, and substrate ____ the fit, which improves _____. * There is a ___ range of ____ specificity..
* flexible, * adjust to maximum, * catalysis. * **greater** range, * **substrate** specificity
35
**The Induced Fit Hypothesis** * Some proteins can ___ their shape (______) * When a **substrate combines** with an ____, it **induces a change** in the **enzyme's** ____ * The **active site** is then ____ into a ____ conformation making the __ **environment suitable** for the reaction * The ____ of the substrate are ___ to make the reaction ___ (lowers activation energy)
* change, (conformation) * enzyme, * conformation * moulded, precise, chemical * bonds, stretched, easier
36
Enzyme Catalyzed Reactions * When a **substrate (S) fits properly in an active site**, an ____ complex is formed: **E + S ⇌ ES** * **Within the active site** of the ES complex, the reaction. occurs to ___ **substrate** **to product (P):** **ES → E + P** * The **products are then ___ **, **allowing another** **substrate molecule** to **___** the enzyme o this cycle *can be repeated millions* (or even more) times per minute * The **overall reaction** for the conversion of substrate to product can be written as follows: **E + S ⇌ ES → E + P**
* enzyme-substrate (ES) * convert: * released * bind
37
**Enzymatic reaction steps**
1) Substrate approaches active site 2) Enzyme-substrate complex forms 3) Substrate transformed into products 4) Products released 5) Enzyme recycled
38
**Enzyme Kinetics** ***Enzyme activity*** can ***be assayed*** in many ways
o disappearance of substrate o appearance of product o continuous assay o end point assay
39
The ___ of an enzyme-catalyzed reaction is dependent upon the ____
velocity (V), substrate concentration [S]
40
at _, . A significant amount of **substrate has not yet been converted to product.**
initial velocity of a reaction
41
at this point, **addition of more substrate will not increase the rate of the reaction**
maximal velocity of a reaction
42
The ___ **describes the kinetic behavior** of many enzymes
Michaelis-Menten equation
43
Michaelis-Menten equation o **maximum rate** that can be observed in the reaction o **substrate is present in excess** o **enzyme can be saturated** (zero order reaction)
at Vmax
44
o a **constant that is related to the affinity of the enzyme** for the substrate o units are in terms of concentration
michaelis constant, Km
45
Enzymes are never expressed in terms of their ____ (as mg or µg etc.) but are expressed only as ____.
concentration, activities.
46
* ____ **moles of substrate converted to product per unit time**. o The **rate** of appearance of ___ or the rate of disappearance of ____ o **Test the absorbance**: __
* Enzyme activity o product, substrate o **spectrophotometer**
47
Factors affecting enzyme activity
* Concentration of substrate * Concentration of enzyme * Temperature * PH * Activators * Inhibitors
48
the **increased in velocity is proportional to the substrate concentration**
Substrate concentration: **non-enzymatic reaction**
49
, a **faster reaction occurs but it reaches a saturation point** when all the enzyme **molecules are occupied**.
substrate concentration: **enzymatic reactions**
50
Elevated alkaline phosphatase levels can indicate **____** (**bile flow obstruction**), *liver disease*, or *bone diseases* such as **_____ disease**
* **cholestasis** * **Paget's disease**