General Biochemistry Flashcards by Franklin Igbokwe

Macromolecules capable of speeding the the rate of a reaction without being used up at the end of the reaction are called __________________

Enzymes

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Enzymes are otherwise called _____________

Biocatalysts

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Enzymes are different from catalysts in the sense that ________________

Enzymes function in a biological system
Catalysts function in a non-living system

Enzymes only speed up the rate of a reaction
Catalysts speed up or slow down the rate of a reaction

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Enzymes can be denatured by changes in ___________ and ______________

Temperature
PH

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Enzymes occur below ____________°C

100

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What is the catalytic power of enzymes?

10⁶ to 10¹²

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Which is true of enzymes
a) Undergo physical changes during a reaction and remain that way at the end of the reaction

b) Undergo no changes at the beginning of a reaction but changes toward the end

c) Undergo physical change during a reaction and changes back to its original form at the end of the reaction

C
Enzymes undergo physical changes during a reaction but revert back to their original forms at the end of the reaction

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Enzymes exhibit their catalytic effects on substances known as _______________

Substrates

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The fundamental structural units of all proteins are __________________

Amino acids

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Peptide bonds are _____________ bonds

Covalent

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Proteins contain __________% of carbon

50-55

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Proteins contain ____________% of nitrogen

15-18

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Name the 10 essential amino acids

Methionine
Arginine
Tryptophan
Threonine
Histidine
Isoleucine
Leucine
Lysine
Valine
Phenylalanine

Mnemonic: vote MATT HILL for VP

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Name the 10 Non-essential amino acids

Alanine
Asparagine
Aspartate
Proline
Serine
Cysteine
Tyrosine
Glycine
Glutamine
Glutamate

Mnemonic: Always Allow Annoying People Sit Close To Gi-Gantic Girls

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Amino acids in nature that do not occur in proteins are called ______________

Non-protein amino acids

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4 physical properties of amino acids

Some are tasteless
Some have sweet flavor
They are white crystalline structures
Soluble in water
Insoluble in non-polar organic solvents
High melting point

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Amino acids contain both acid and base and can react with both of them to give water.
This is the ________________ nature of amino acids

Amphoteric

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Amino acids with both negative and positive charges are called ____________

Zwitterions

**Tip: Remember “Twitter Ions”

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The PH where amino acids have no tendency to move to a positive for negative electrode is called ______________

Isoelectric PH

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Peptide bonds are formed between _________________

The carboxylic group of one amino acid and the amino group of the other

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A typical amino acid has 5 components

Central carbon
A- Amino group
R- Group (Side chain)
C- Carboxylic group
H- Hydrogen atom

Mnemonic: Carbon - ARCH

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Amino acid structures differ due to differences in their ____________

Side chains

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________________ is a commonly occurring tripeptide found in living organisms used for detoxification purposes

Gluthatione

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______________ is a nanapeptide in the body that induces labor in pregnant women

Oxytocin

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____________ is a nanapeptide in the body that controls blood pressure

Vasopressin

______________________ is a Dipeptide commercially used as a sweetener for diabetics

L-Aspartyl-L-phenylalanine

What are the building blocks of proteins?

Amino acids

The physiological PH of amino acid is ___________

7.4

Proline is the only __________ amino acid

Cyclic

Aromatic amino acids are _______________, ______________ and _____________

Phenylalanine Tyrosine Tryptophan Mnemonic: Pray Ten Times

Aliphatic amino acids are _______, __________, ____________, ___________, ______________

Glycine Leucine Alanine Valine Isoleucine Mnemonic: GLAVI

A peptide formed between 2 amino acids is called _______________

Dipeptide

A peptide formed between 3 amino acids is called _______________

Tripeptides

A peptide formed between a few amino acids is called _______________

Oligopeptides

A peptide formed between many amino acids is called _______________

Polypeptide

__________ amino acid forms hormones like adrenaline, norepinephrine, thyroid hormones and melanin

Tyrosine

Amino acids that are converted to carbohydrates are called_______________

Glycogenic amino acids

Niacin is Vitamin B3 and it is synthesized by what amino acid?

Tryptophan

____________ and ___________ amino acids help in the synthesis of bile salts

Glycine Cysteine

Serotonin is formed from which amino acid?

Tryptophan

_____________ amino acid is used for the synthesis of haem

Glycine

Histidine turns to _____________ upon decarboxylation

Histamine

Cysteine and methionine are sources of _____________

Sulfur

Substances derived from amino acids are called _____________

Amino acid derivatives

Gluthatione Betaine Alpha-ketoglutarate Histamine Dopamine GABA The above are examples of ____________

Amino acid derivatives

What type of amino acid can be synthesized in the body a) Essential b) Semi-Essential c) Non-Essential

Non-Essential amino acids

Oligosaccharides contain _____________ monosaccharides

2-10

'Two monosaccharides joined covalently by an O-glycosidic bond' The above is a ______________

Disaccharide

Disaccharides are homogenous and not heterogeneous True/False

False Disaccharides can both be homogeneous as seen in maltose and heterogenous as seen in sucrose and lactose

What are enzymes?

Enzymes are proteins that alter the rate of a metabolic reaction in a biological system while not being used up at the end of the reaction.

Enzymes function in a biological system as ________________ function in a non-living system

Catalysts

Enzymes are otherwise called ________________

Biocatalysts

Enzymes can be denatured by change in _______________ and _______________

PH and Heat

Enzymes occur below ___________°C

100

What is the catalytic power of enzymes?

10⁶ - 10¹²

Enzymes exhibit their catalytic effects on substances called _____________

Substrates

Enzymes are said to exhibit Absolute specificity in what situation?

When they catalyze only one particular reaction

_____________________, ____________________, and __________________ are specificity of enzymes

Absolute Group Optical

Enzymes are said to exhibit Group specificity in what situation?

When they act on substrates with a specific functional group

Enzymes are said to exhibit optical specificity in what situation?

When enzymes are specific to the substrates and their optical configurations

Cite an example of Optical specificity

L-amino oxidase acting on L-amino acid but not on D-amino acid. D-glucose oxidase acting on D-glucose but not on L-glucose L-lactate dehydrogenase acting on L-lactic acid but not on D-lactic acid

Cite an example of Group specificity of enzymes

Pepsin Trypsin Chymotrypsin

Cite an example of Absolute specificity

Glucokinase acting on glucose to form glucose-6-phosphate

Enzymes are classified into 6 in what order

Oxidoreductases Transferases Hydrolaces Lylases Isomerases Ligases Mnemonic: **OTHLIL**

Enzymes that catalyze oxidation and reduction reactions are classified as ________________

Oxidoreductases

Enzymes that _____________________ are classified as transferases

Catalyze transfer of chemical groups from one compound to another

Enzymes that catalyze the hydrolysis of a bond are classified as _______________

Hydrolaces

Lylases are enzymes that _________________

Catalyze the breaking down if a bond without catalysis

Enzymes that catalyze the formation of an isomer of a compound are classified as ________________

Isomerases

Ligases are enzymes that catalyze ____________________

The association of two molecules

The minimum extra energy required by a reactant to get converted to a product is termed _______________

Activation energy

State Fischer's Lock and Key theory?

The active site of an enzyme has a conformational shape that compliments the shape of the binding substrate

What is the active site of an enzyme?

This is the part of the enzyme where substrate molecules bind and a chemical reaction takes place.

What is the Allosteric site of an enzyme?

This is the part of an enzyme that inhibits the activity of the enzyme by changing the conformational shape of the active site.

State Koshland's induced-fit theory

The active site of an enzyme will undergo a conformational change to attain an optimal fit for the binding substrate. It is an enzyme-substrate interaction.

The protein part of an enzyme is called ____________

Apoenzyme or Apoprotein

A complete active enzyme is called __________________

Holoenzyme

The non-proteinous parts of an enzyme are called _________________

Co-factors

The non-proteinous part of an enzyme are of two types. __________________ and _______________

Organic part called Coenzymes Inorganic part called Ions

What are metalloenzymes?

These are enzymes with a definite amount of metal ions that are retained throughout

What are isoenzymes?

These are enzymes that exist in different forms within a single cell or species of an organism

Isoenzymes are otherwise called ________________

Isozymes

5 uses of enzymes

Laundry Beverages Altering metabolic reactions Diagnosis of diseases Used in drug and pharmaceutical companies Used in manufacturing industries

What are nucleotides?

Building blocks of amino acids

Nitrogenous base + Ribose = ? The above reaction would yield a _______________

**Nucleoside**

Nitrogenous base+ Ribose + Phosphate group= ? The above reaction would yield a __________________

Nucleotide

_________________ and _________________ are nitrogenous bases that make up nucleotides

Purine Pyrimidine

The major bases of Purine are?

Adenine Guanine

The major bases of pyrimidine are?

Cytosine Uracil Thymine

The minor bases of purine are?

Xanthine Hypoxanthine

What is a Ribose?

A Ribose is a 5 carbon sugar that helps differentiate between DNA and RNA

___________________ base is formed from a hexagonal and pentagonal structure

Purine Tip* Number the structure in an anticlockwise manner from 10 o'Clock and then clockwise from 12 o'Clock

______________ is formed from adding an amino group to position 6 of the Purine parent structure

Adenine Tip* NH² signifies an Amino group

Guanine is formed from oxidizing position _______ and adding an amino group to position _______ of the parent structure

Oxidizing position 6 Amino group to position 2 Tip* NH² signifies an amino group O denotes oxidization The oxidant collects the double bond

________________ base is formed from a hexagonal structure

Pyrimidine Tip* Structure is numbered in a clockwise manner from 6 o'Clock

Cytosine structure is formed from the pyrimidine parent structure by _______________

Oxidizing position 2 Adding an amino group to position 4

____________________ structure is formed by oxidizing both positions 2 and 4 and methylating position 5 of the pyrimidine parent structure

Thymine

___________________ structure is formed from oxidizing positions 2 and 4 of the pyrimidine parent structure

Uracil

General Biochemistry Flashcards

(98 cards)