enzyme Flashcards

(34 cards)

1
Q

He coined the term “enzyme” in 1878

A

Friedrich Wilhelm Kuhne

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2
Q

“biological catalysts” that had previously been called

A

ferments

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3
Q

 The word itself means ‘in yeast’ from the Greek word ___
“en” means in “zyme” means ___ or ___

A

enzymos
yeast or leaven

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4
Q

who prepared malt extract from germinating barley seeds

A

Dubrunfaut

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5
Q

___ and ____prepared an enzyme, the diastase (now knows as ___) from malt extract.

A

Payen and persoz
amylase

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6
Q

He prepared a substance from germinating wheat, which acted like diastase

A

Horace de Saussure

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7
Q

He succeeded in extracting pepsin and later trypsin

A

Theodor Schwann

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8
Q

He was recognized with remarkable foresight the catalytic nature

A

Jõnes Jacob Berzelius

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9
Q

He demonstrated that alcoholic fermentation was brought about by the action of living yeast cells

A

Pasteur

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10
Q

at Cornell University, isolated and purified an enzyme, the urease, from jack bean (canavalia ensiformis ), thus confirming the proteinaceous nature of the enzymes

A

James B. Sumner

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11
Q

The human body makes approx. ___ digestive enzymes.

A

22

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12
Q

 It is a protein molecule that functions as a catalyst to speed up chemical reactions in living organisms.

A

Enzyme

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13
Q

 Speeds up chemical reactions. They catalyse nearly all the chemical reactions taking place in the cells of the body.

A

Biological Catalysts

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14
Q

Used in multiple reactions. It can not be altered or consumed during the reaction. They remain unchanged after each reaction and can therefore be reused.

A

Reusable

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15
Q

 One type of enzyme for one type of reaction.

A

Specific

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16
Q

 Each enzyme is characterized by a code no. called Enzyme Code no. or EC number and contain four figures (digits) separated by a dot.

A

Systemic Name

17
Q

 The molecules that bind to the enzyme are called

18
Q

The location where they bind (sit down) is called the

19
Q

Lock-and-Key Model
 Proposed by

A

Emil Fischer in 1894

20
Q

Induced-Fit Model
 Proposed by _____

 The active site is flexible, not rigid.
 The shapes of the enzyme, active site, and substrate adjust to maximize the fit, which improves catalysis.
 There is a greater range of substrate specificity.

A

Danial Kosh Lan in 1958

21
Q

Occur when molecules interact and chemical bonds between them are formed or broken.

A

Chemical Reactions

22
Q

 The ___ or ___ a measurement of how fast a reaction occurs.

A

rate of reaction or reaction rate

23
Q

 It is the energy required for a chemical reaction to occur.

A

Activation Energy

24
Q

 the change of folding structure of a protein (and thus of physical properties) caused by heating, changes in pH, or exposure to certain chemicals

25
 It is an increase in the rate of reaction with the help of enzyme (as catalyst)
Enzyme Catalysis
26
 is one of the simplest and best-known models of enzyme kinetics. It is named after ___ and ___. This model is based on the single substrate reaction:
Leonor Michaelis and Maud Menten Michaelis-Menten kinetics
27
substances which alter the catalytic action of the enzyme and consequently slow down, or in some cases, stop catalysis. This effect may be permanent or temporary
Inhibitors
28
 An inhibitor may bind to an enzyme and block binding of the substrate, for example, by attaching to the active site. The inhibitor “competes” with the substrate for the enzyme. That is, only the inhibitor or the substrate can be bound at a given moment.  Chemicals that resemble an enzyme’s normal substrate and compete with it for the active site.  Reversible depending on concentration of inhibitor and substrate.
Competitive Inhibitor
29
 An inhibitor that doesn't block the substrate from binding to the active site. Instead, it attaches at another site called “allosteric site” and blocks the enzyme from doing its job. This inhibition is said to be "noncompetitive" because the inhibitor and substrate can both be bound at the same time.  Do not enter active site, but bind to another part of the enzyme, causing the enzyme & active site to change shape.  Usually reversible, depending on concentration of inhibitor & substrate.
Noncompetitive inhibitor
30
, is just any form of regulation where the regulatory molecule (an activator or inhibitor) binds to an enzyme someplace other than the active site. The place where the regulator binds is called the ____
Allosteric Regulation allosteric site
31
decrease the activity of an enzyme
Inhibitors
32
increase the activity of an enzyme
Activators
33
Other enzymes contain a nonprotein component called a _____ that is necessary for the enzyme’s proper functioning. There are two types of cofactors: inorganic ions [e.g., zinc or Cu(I) ions] and organic molecules known as ______.
cofactor coenzymes
34
prepares the active site for catalytic activity.
Coenzyme