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LIPOIC ACID HAS ITS UNIQUE STRUCTURE
M.U.Djalilov O.S,Tashanov
Samarkand State Medical University
mustafoevakmal@gmail.com
Annotatsiya. Lipoic acid, entering the tissues, binds covalently to the NH2 group
of lysine of the active site of the apoenzymes of "lipoic" enzymes. These include multi-
enzyme complexes that carry out keto acid reactions.
Keywords:
Metabolism,
Biological
role,
HS-CoA
and
NAD+,
lipoacetyltransferase, lipoacetyltransferase
Sources of lipoic acid are yeast, meat products, and milk. In the 1950s, lactic
acid bacteria growth factor was isolated from yeast and liver tissue, which is not related
to any of the known vitamins; some species of streptococci also needed it as a growth
factor. In crystalline form, this factor was identified with α-lipoic acid (1,2-dithiolan-
3-valeric) (Fig. 3):
Rice. H. Diagram of the redox reaction of lipoic acid
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As you can see from these formulas, lipoic acid can exist
Thanks to which its coenzyme functions are realized
Metabolism.
Lipoic acid, entering the tissues, binds covalently to the NH2 group
of lysine of the active site of the apoenzymes of "lipoic" enzymes. These include multi-
enzyme complexes that carry out keto acid reactions.
Biological role
. Lipoic acid plays the role of a prosthetic group along with
thiamine pyrophosphate and HS-CoA in a complex multienzyme pyruvate and α-
ketoglutarate-dehydrogenase systems
Pyruvate dehydrogenase multienzyme complex has a complex structure, its
molecular weight is 5.3*10
6
Yes, it includes enzyme and cofactors:
•
the first enzyme, pyruvate decarboxylase (K.F.1.2.4.1.) consists of 12
dimeric molecules, each of which has 2 molecules of thiamine pyrophosphate attached,
which act as coenzymes;
•
the second enzyme is lipoacetyltransferase (K.F.2.3.1.12.), the enzyme is
concentrated in the central part of the B complex in the form of 24 molecules packed in
the shape of a cube, each B molecule as a prosthetic group contains a lipoic acid residue
connected to the apoenzyme via e-aminogrupe lysine; This compound provides lipoic
acid with motility as part of a multienzyme complex and contact with pyruvate
decarboxylase and dihydrolipoyl dehydrogenase;
•
the third enzyme is dihydrolipolyl dehydrogenase (K.F.1.8.1.4.), the
enzyme consists of 6 dimeric molecules containing 2 molecules of FAD as a coenzyme
•
In addition to the listed enzymes and their cofactors, the complex includes
two external coenzymes: HS-CoA and NAD+
The spatial organization of the components of the complex is very important for
catalysis. Lipoic acid, due to its specific structure, is very mobile and is capable of
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forming a bond with the lysine residue of the second enzyme (lipoacetyltransferase). In
the process of catalysis, the "handle" of lipoamide moves between the first (pyruvate
decarboxylase) and the third (dihydrolipoyl dehydrogenase) enzyme. In this way,
lipoamide can react both in the B-bound thiamine pyrophosphate and soluble coenzyme
A, as well as with the electron-accepting FAD in the third enzyme. The protein part of
acetyltransferase, which binds lipoic acid, is very mobile, and this increases the "range"
of action of the lipoamide "pen".
The general equation of oxidative decarboxylation of pyruvate is as follows:
α-ketoglutarate dehydrogenase complex is similar to pyruvate dehydrogenase in
mechanism of action and structure, but differs in the structure of apoenzymes.
Lipoic acid plays an indispensable role in the oxidation and transport of acyl
groups in multicomponent enzyme systems. Its main function is direct participation in
oxidative decarboxylation in tissues of α-keto acids (pyruvic and a-ketoglutaric acids).
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