Enzymes The classification and nomenclature. Lyases and Transferases
The plan of lecture
The classification of and nomenclature of enzymes
The nomenclature of enzymes
General characteristic and classification of transferases
The structure and catalytic role of aminotransferases
The importance of transamination
The structure and catalytic role of methyltransferases
The structure and catalytic role of acyltransferases
The structure and catalytic role of phosphotransferases
General characteristic and classification of Lyases
The structure and catalytic role of decarboxylases of amino acids
The structure and catalytic role of decarboxylases of ketoacids
The structure and catalytic role of Carbonic anhydrase
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Category: chemistrychemistry

Enzymes The classification and nomenclature. Lyases and Transferases

1. Enzymes The classification and nomenclature. Lyases and Transferases

2. The plan of lecture

• 1) The classification and nomenclature of
enzymes
• 2) Transferases, representatives –
structure and catalytic role
• 3) Lyases, representatives – structure and
catalytic role

3. The classification of and nomenclature of enzymes

I. Oxireductases (ОR) catalyze oxidativereductive reactions (ОRR);
II. Transferases catalyze the transfer of
atoms groups from one substrate to
another

4.

III. Hydrolases catalyze the cleavage of
complex substances to simple ones with
participation of water (this process is called
as hydrolysis)

5.

IV. Lyases catalyze the reactions of
cleavage without water or promote the
addition of atoms groups in the site of
double or triple bonds

6.

V. Isomerases catalyze the isomerizm
ведут реакции изомеризации;
VI. Lygases, or synthetases catalyze the
synthesis of some substances

7. The nomenclature of enzymes

Each class is divided into subclasses (from
4-13), subclass is divided into
subsubclasses, each subsubclass
contains a representative

8.

Therefore the cipher of each enzyme
consists of 4 numbers: first one shows the
number of class; second one indicates
number of subclass, third one represents
the number of subsubclass, fourth one
shows the place of a representative in
subsubclass

9.

For instance, the cipher for pancreatic lipase
is 3.1.1.3., this is means that pancreatic
lipase refers to hydrolases (3-rd class, that
is catalyzes the hydrolysis)

10.

To the 1-st subclass (esterase, that is
catalyzes the hydrolysis of ester bonds), to
the 1-st subsubclass (that is catalyzes the
hydrolysis of ester bonds formed by
carboxylic acids), the place in subsubclass
is third one

11. General characteristic and classification of transferases

Transferases are enzymes which catalyze the reactions of
transfer of groups of atoms from one substrate to
another.
Almost all transferases are two-component enzymes. They
are contained in the cells only.
On the depend on character of transported groups there
are some subclasses of transferases: amino-, methyl-,
acyl- and phosphotransferases

12. The structure and catalytic role of aminotransferases

Coenzyme of aminotransferases is phosphopyridoxal (vitamin B6 + H3PO4)
О
С Н
СН2 – О – Р
НО
Н3С
N
Aminotransferases catalyze the reactions of transport of amino groups from
amino acids to ketoacids that results in formation of non-essential amino
acids (transamination)
СН3
COOH АLАT
CH3
COOH
СНNH2 +
CH2
C=O
+
CH2
COOH
CН2
COOH
CH2
C=O
CHNH2
СООН
COOH
АLА
Pyruvate
α КG
GLU

13. The importance of transamination

1)
2)
3)
4)
This is a pathway of synthesis of non-essential amino acids;
This is the way of integration of metabolism of carbohydrates and
amino acids due to reversibility of transamination
This is initial state of amino acids catabolism
Aminotransferases are organospecific enzymes, e.g. alanine
aminotransferase occurs mainly in liver; aspartate
aminotransferase does in liver, myocardium, muscles. This has a
diagnostic role, because in lesion of these organs and tissues the
activity of these enzymes is increased in blood plasma. It is due to
exit of them from corresponding cells into blood

14. The structure and catalytic role of methyltransferases

Coenzyme is reduced form of Folic Acid (vitamin
Bc) – tetrahydrofolic acid (THFA). It is reduced
residue of pteridine, para-aminobenzoic and
glutamic acids.
Methyltransferases catalyze the reactions of
intermolecular transport of methyl- and other
one-carbon groups (methylation). The source
of methyl group is methionine (Met). In these
reactions vitamin B12 is also necessary.

15.

OH
H
N
HO
N
+
СН2 – S – CH3
CH2
CHNH2
COOH
Met
OH
CH3
+
N
ТHFA
v. B12
N
CH2SH
CH2
CHNH2
COOH
HO
Uracil
Thymine
СН2 – ОН
СН2 – NH2
CH2 – OH
CH2 – N
+3CH3
ТHFA,v. B12
Ethanolamine
CH2NH2
CHOH
+ CH3
CH3
CH3
Choline
CH3
CH2 NH – CH3
CHOH
ТHFA,v. B12
OH
OH
Noradrenalin
OH
OH
Adrenalin
Homocysteine

16. The structure and catalytic role of acyltransferases

Coenzyme is HSCoA (coenzyme of acylation). It consists
of adenosine-3-monophosphate, 2 residues of
phosphoric acid, pantothenic acid (vitamin B3) and
thioethylamine.
Acyltransferases catalyze the reactions of transport of
residues of carboxylic acids, e.g. residues of acetic
acid (hence, their name – acetyltransferases)
R
AТP
CH2
COOH
Fatty acid
АМP + РР
R
CH2
C=O
S
SCoA
active FA

17. The structure and catalytic role of phosphotransferases

Phosphotransferases, or kinases are one-component enzymes, but
consist of some subunits, i.e. these enzymes have quaternary
structure.
Phosphotransferases catalyze the reactions of transport of residues of
phosphoric acid (phosphorylation).
When phosphoric acid is attached to substrate. The product becomes
more active, therefore these enzymes are also named as kinases
The sources of phosphoric acid are:
1)
ATP;
2)
High energetic phosphorus-containing substrates

18.

ATP is more often source of phosphoric acid. The residue of phosphoric acid
may be transported on substrate with conservation of macroergic bond
(reversible phosphorylation) and without its (irreversible phosphorylation)
H2N
C = NH
N – CH3
CH2
COOH
Creatine
СН2ОН
НО
ОН
Glucose
ОН
ОН
АТP
АDP
Creatine kinase
АТP
АТP
АDP
HN PO3H2
C = NH
N – CH3
CH2
COOH
Creatine phosphate
СН2О – РО3Н2
АDP
Glucokinase
ОН
ОН
ОН
Glucose-6-phosphate
НО

19.

The source of phosphoric acid can be a phosphorus-containing high
energetically substrate. In this case the reaction will be named as
substrate phosphorylation:
СOOH
C O PO3H2
CH2
АDP
Phosphoenolpyruvate
АTP
Pyruvate kinase
COOH
C – OH
CH2
Enolpyruvate

20. General characteristic and classification of Lyases

This class of enzymes includes enzymes which
catalyze the reactions of cheeping off (removal)
of some groups of atoms (CO2, NH2, etc) or
addition of them to the place of multiple bonds.
Accordingly to removed groups they’re named
(decarboxylases, deaminases, etc)
Subclass of decarboxylases includes two
subsubclasses – decarboxylases of amino- and
keto acids

21. The structure and catalytic role of decarboxylases of amino acids

Coenzyme of these enzymes is phosphopyridoxal (vitamin B6+H3PO4)
– CH2 – CH2
N
– CH2 – CH – COOH
N
NH2
NH2
– СО2
NH
His
NH
Histamine

22. The structure and catalytic role of decarboxylases of ketoacids

These are two-component enzymes. Coenzyme is thiamindiphosphate (vitamin B1
+ 2H3PO4)
NH2
CH3
CH2
N
N
O
H3C
O
CH2 – CH2 – O – P – O – P – OH
N
S
OH
OH
Pyruvate decarboxylase catalyzes the decarboxylation of
pyruvate, which results in formation of active acetic acid
СН3
СН3
NАD
NADН2
С=О
С=О
PDH
СООН Аc/tr
SCoA
PDC
Oxidative
HSCoA
Pyruvate
СО2
Active
acetic acid
decarboxylation

23. The structure and catalytic role of Carbonic anhydrase

This is a two-component enzyme. Zinc is a
constituent of coenzyme. The enzyme catalyzes
the reaction of synthesis and cleavage of
carbonic acid:
Н2О + СО2
Н2СО3
The direction of reaction depends on concentration
of CO2, therefore this enzyme takes part in
regulation of respiratory center
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