Mod.A. Bio Lec1: Enzymes Flashcards

1
Q

Enzymes are:

A

are complex protein : composed of protein PLUS a nonprotein

  • الجزء البروتيني → يسمى Apoenzyme * الجزء الغير بروتيني → يسمى Prosthetic group / Coenzyme / Cofactor
  • دورها : biological catalysts.: Increase the rate of reaction by lowering the energy of activation.
  • أثناء التفاعلات : 1- are neither consumed nor produced during the reaction.

2- catalyze energetically feasible reactions only. بمعنى أن هناك تفاعل واحد قابل للتنفيذ

  • التخصصية : often show a high specificity
    toward one substrate

Enzyme Specificity Types :
1- Absolute 2- Group 3- Linkage

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2
Q

Active site

A

where binding with a substrate takes place

  • Including
    1- contact site for binding a substrate and

2- catalytic site

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3
Q

Allosteric site

A

المادة المرتبطة:- Allosteric Regulator :

وهي molecules structurally dissimilar substrate bound to this site

  • نتيجة ارتباطها could change the enzyme configuration
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4
Q

ENZYME REGULATION is by

A

1- allosteric regulation

2- covalent modification

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5
Q

ALLOSTERIC REGULATION

A

Allosteric regulation occurs when a non-substrate molecule ( تسمى Allosteric regulators ) binds or modifies an allosteric site, which is a site other than the active site

  • Allosteric regulators can be inhibitors or activators .
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6
Q

COVALENT MODIFICATION

A
  • كيف تتم : typically occurs by the addition of a phosphate group to one or more of the
    enzymes amino acids
  • النتيجة : if the phosphate is added in a hydrophobic region of the enzyme,

1- it makes that region hydrophilic. because phosphate carries a negative charge.

2- The protein twists, thereby inducing the enzyme to change its shape.
and this can expose or hide the active site. بمعنى The shape change can result in the activation or inactivation of an enzyme.

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7
Q

How does substrate concentration affect enzymatic activity ?

A

at constant enzyme concentration :

The rate of reaction increases as substrate concentration increases

Maximum activity occurs when the enzyme is saturated.

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8
Q

Km

A

is the substrate concentration at which the reaction rate is half of Biochemical reactions

Km describes an affinity of the enzyme to its substrate :
indirect proportionality العلاقة بينهما علاقة عكسية

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9
Q

Clinical utility of enzymes:

A

1- Diagnosis and follow up of diseases

( Non Functional Plasma enzymes)

2- Therapeutic agents

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10
Q

FACTORS DETERMINING CLINICAL UTILITY

A

1- Organ and tissue distribution of enzymes

2- Intracellular localization of enzymes

3- Timing and magnitude of elevation

4- Way of enzyme elimination from blood

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11
Q

Enzyme increases are usually related to

A

leakage of enzymes from damaged cells

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12
Q

Enzyme assays are done by :

A

1- the catalytic activity of the enzyme (most used)

2- the concentration of the enzyme

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13
Q

Katal (catalytic activity)

A

is the number of mole of substrate transformed
per second per litre of sample.

وحدة قياسها : International Unit ( U/L ) .

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14
Q

Amylase and lipase indicate :

A

Pancreatitis

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15
Q

Acid phosphatase indicates :

A

Prostate cancer

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16
Q

Alk.phosphatase indicates :

A

Bone , liver diseases and hyperparathyroidism

17
Q

Creatine kinase indicates :

A

myocardial infarction

18
Q

Lactate DH. indicates:

A

myocardial infarction liver diseases, Leukemia

19
Q

Transaminases

( ALT & AST ) indicate :

A

myocardial infarction(SGOT) liver diseases(SGPT)

20
Q

Hemolysis of the blood sample lead to

A

increase of RBCs intracellular enzymes; LDH, AST, ALT…..

21
Q

Strenuous exercise prior to the test shows:

A

increase of LDH

22
Q

Streptokinase:

A

Enzyme prepared from streptococcus

  • استخدامه : Used in clearing blood clots in
    myocardial infarction

كيف تقوم بهذا الدور ؟
Act by activating plasminogen to form plasmin.

النتيجة : Plasmin cleaves fibrin into
several soluble products