Презентация, доклад Enzymes The classification and nomenclature. Lyases and Transferases


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Презентации» Химия» Enzymes The classification and nomenclature. Lyases and Transferases
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Enzymes The classification and nomenclature. Lyases and Transferases

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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


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The classification of and nomenclature of enzymes I. Oxireductases (ОR) catalyze oxidative-reductive reactions (ОRR); II. Transferases catalyze the transfer of atoms groups from one substrate to another

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

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

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

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

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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 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

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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) 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)

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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 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

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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

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The structure and catalytic role of aminotransferases Coenzyme of aminotransferases is phosphopyridoxal (vitamin B6 + H3PO4) 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 CH3 COOH СНNH2 + CH2 C = O + CH2 COOH CН2 COOH CH2 C = O CHNH2 СООН COOH

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The importance of transamination 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

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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.

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СН2 – S – CH3 CH2SH + CH2 + CH2 CHNH2 CHNH2 COOH COOH Met СН2 – ОН +3CH3 CH2 – OH СН2 – NH2 CH2 – N CH3 CH3 CH3 CH2NH2 CH2 NH – CH3 CHOH + CH3 CHOH

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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 АМP + РР R CH2 CH2 COOH C = O Fatty acid S SCoA active FA

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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: ATP; High energetic phosphorus-containing substrates

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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) 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 HN PO3H2 C = NH АТP АDP C = NH N – CH3 N – CH3 CH2 CH2 COOH COOH СН2ОН СН2О – РО3Н2

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

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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

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The structure and catalytic role of decarboxylases of amino acids Coenzyme of these enzymes is phosphopyridoxal (vitamin B6+H3PO4)

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The structure and catalytic role of decarboxylases of ketoacids These are two-component enzymes. Coenzyme is thiamindiphosphate (vitamin B1 + 2H3PO4) Pyruvate decarboxylase catalyzes the decarboxylation of pyruvate, which results in formation of active acetic acid СН3 СН3 С = О С = О СООН SCoA

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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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