MODULE 9 FIG.
1 ENZYME COMPLEX
ENZYMES
(Nomenclature and Classifications of Enzymes)
LEARNING TARGETS:
At the end of the module, students will be able
to:
1. Define and know the importance of enzyme
in our body;
2. Identify the nature enzymes;
3. Name the different structures of enzymes;
• SUBSTRATE - any substance that reacts to the
4. Identify the salient features of co-enzymes;
5. Enumerate enzymes containing metals; active site of an enzyme
6. Explain how enzymes are named; and, • CATALYTIC SITE/ACTIVE SITE - The specific
7. Identify the different classification of region of an enzyme where a substrate binds
enzymes. and catalysis takes place or where chemical
reaction occurs
• APOENZYME - protein portion of an enzyme
(inactive)
• COFACTOR - non-protein part of an enzyme
ENZYMES (activator)
• Enzymes are built of proteins folded into
• HOLOENZYME – Apoenzyme + Cofactor
complicated shapes, they are present
• ZYMOGEN/PROENZYME - An inactive enzyme
throughout the body
precursor that requires a biochemical change to
• They bind to molecules and alter then in become active or functional
specific ways Ex: Pepsinogen – inactive form of pepsin
• They are essential for respiration, digesting • PRECURSOR - a substance from which
food, muscle and nerve function, among another, usually more active
thousands of other roles or mature substance is formed.
• The chemical reactions that keep us alive – Ex: Vit. B5 – precursor of Coenzyme A
our metabolism- rely on the work that
enzymes carry out
• Enzymes speed up (catalyze) chemical
reactions; in some cases, enzymes can
make a chemical reaction millions of times
faster than it would have been without it.
• They breakdown large molecules into
smaller substances that can be easily
absorbed by the body.
The functions of enzymes include, but are not
limited to;
• Digestive system – enzymes help the body
break down larger complex molecules into
smaller molecules.
Ex: Pepsin – digestion of protein • Coenzyme – cofactors that are small
organic molecule
• DNA replication – each cell in the body Ex:
contains DNA. Each time a cell divides, that a) FAD - Flavine Adenine Dinucleotide
DNA needs to be copied. Enzymes help in b) NAD – Nicotinamide Adenine Dinucleotide
this process by unwinding the DNA coils c) FMN – Flavine Mononucleotide
and copying the information. • Inorganic/Metal ion – also a most common
Ex: DNA helicases – unwinding of DNA cofactor
• Prosthetic group – cofactors that are
• Liver enzymes – the liver breaks down tightly bound
toxins in the body. To do this, it uses a • Cosubstrate - cofactors that are loosely
range of enzymes bound
Ex: Ornithine carbamoyltransferase • Metalloenzyme – enzymes with ion
– ammonia to urea cofactor that is tightly bound
• Metal-activated enzymes - enzymes with
ion cofactor that is loosely bound
COENZYME PRECURSOR
DEFICIENCY • choline esterase/cholinesterase –
DISEASE
acetyl choline to acetic acid and
Coenzyme A Vit. B5 Dermatitis
Growth choline
FAD, FMN Vit. B2 c) Nucleases – aid in the hydrolysis of
retardation
NAD, NADP Vit. B3 Pellagra nucleic acids
Thiamine
Vit. B1 Beriberi • polynucleotidases – nucleic acid to
pyrophosphate nucleotides
Megaloblastic
Tetrahydrofolate Vit. B9
anemia
• nucleotidases – nucleotides to
Deoxyadenosyl Pernicious nucleosides and phosphoric acid
Vit. B12
cobalamin anemia • nucleosidase – nucleosides to sugar
Pyridoxal and purine or pyrimidine
Vit. B6 Dermatitis
phosphate d) Amidases – aid in the hydrolysis of
amides
NOMENCLATURE OF ENZYME • ureases – urea to ammonia and CO2
• International Union of Biochemistry and • arginase – arginine to ornithine and
Molecular Biology (IUBMB) in 1964, (modified in urea
1972 and 1978), suggested the IUBMB system e) Proteases – aid in the hydrolysis of
of nomenclature of enzymes. As per this system, proteins
the name starts with EC (enzyme class) followed • pepsin – proteins to proteoses and
by 4 digits. peptones
1) First digit represents the class
• trypsin – cleaves the polypeptide
2) Second digit stands for the subclass
chain from the carboxyl end of
3) Third digit is the sub-sub class or arginine and lysine
subgroup
• chymotrypsin – cleaves the
4) Fourth digit gives the number of the
polypeptide chain from the carboxyl
particular enzyme in the list.
end of phenylalanine, tyrosine and
EX: EC 1.1.1.2 (Alcohol Dehydrogenase)
tryptophan
CLASS NAME EXAMPLE
• rennin – casein to paracasein
1 Oxidoreductases Dehydrogenases, Oxidases, • cathepsin – proteins to proteoses and
Reductases peptones
2 Transferases Transaminases, Kinases • bromelin/bromelain – proteins to
3 Hydrolases Lipases, Proteases, proteoses and peptones
Amylases, Nucleases
f) Peptidases – hydrolyze peptides to
4 Lyases Decarboxylase,
Deaminases, Dehydratases, simple peptides and amino acids
Hydratases • aminopolypeptidases – sequentially
5 Isomerases Isomerases, Mutases cleave the polypeptide chain from the
6 Ligases Synthetases, Carboxylases amino terminal
• carboxypolypeptidases – sequentially
CLASSIFICATION OF ENZYMES ACCORDING cleave the polypeptide chain from the
TO CHEMICAL REACTION CATALYZED: carboxyl terminal
• prolinase – polypeptides containing
I. ADDITION OF WATER MOLECULES praline to simpler peptides and
A. HYDROLASE praline
a) Carbohydrase – aid in the hydrolysis of • dipeptidases – dipeptides to amino
carbohydrates acids
• alpha amylase – starch & glycogen
to dextrin II. TRANSFER OF ELECTRONS
• beta amylase – starch & glycogen to A. OXIDASES – are enzymes which catalyze
dextrin & maltose the removal of hydrogen from a substrate
• lactase – lactose to glucose and and pass it directly to oxygen
galactose a) Dehydrogenases – activate H atoms of
• maltase – maltose to glucose organic compounds
• sucrase – sucrose to glucose and b) Catalase – acts on hydrogen peroxide
fructose to give water and oxygen
b) Esterases – aid in the hydrolysis of c) Peroxidases – act on organic peroxides
esters giving nascent oxygen
• lipases – glycerides to fatty acids d) Tyrosinase – acts on tyrosine
and glycerol e) Ascorbic acid oxidase – acts on
• phosphatase – organic phosphates ascorbic acid
to phosphoric acid
III. SPLITTING OR FORMING A C-C BOND
A. DESMOLASES – catalyze the linkage not
broken by water; splitting or forming a C-C
bond
a) Decarboxylases
• carboxylase – alpha keto acids to
CO2 and aldehydes
• carbonic and anhydrase – carbonic
acid to water and carbon dioxide
IV. TRANSFER OF A RADICAL
A. TRANSAMINASES – catalyze the transfer
of amino groups from amino acids to
ketoacids and thus promote the formation of
new amino acids
• alanine transaminase
• glutamate transaminase
