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JESSA S. ARIÑO
                                    BSE-3B
Central Bicol State University of Agriculture
   Enzymes are most commonly named by
    using a system that attempts to provide
    information about the function rather than
    the structure of the enzyme.
   Type of reaction catalyzed and substrate
    identity are focal points for the
    nomenclature.
   A substrate is the reactant in an enzyme-
    catalyzed reaction.
1.   The suffix –ase identifies a substance as an
     enzyme. The suffix –in is still found in the
     name of the first enzymes studied such as
     trypsin, chymotrypsin, and pepsin.
2.   The type of reaction catalyzed by an
     enzyme is often noted with a prefix.
            oxidase- catalyzes oxidation
     reaction
            hydrolase- catalyzes a hydrolysis
     reaction
3. The identity of the substrate is often noted
  in addition to the type of reaction.
glucose oxidase- catalyzes oxidation of
  glucose
lactate dehydrogenase- catalyzes the
  removal of hydrogen from lactate ion.
Infrequently, the substrate but not the
  reaction type is given:
Urease- catalyses the hydrolysis of urea
Lactase- catalyses the hydrolysis of lactose
According to the International union Of
 Biochemistry an enzyme name has two
 parts:
        -First part is the name of the
 substrates for the enzyme.
        -Second part is the type of reaction
 catalyzed by the enzyme. This part ends
 with the suffix “ase”.
Example: Lactate dehydrogenase
The International Union of Biochemistry and
 Molecular Biology have developed a
 nomenclature for enzymes, the EC
 numbers; each enzyme is described by a
 sequence of four numbers preceded by
 "EC". The first number classifies the
 enzyme based on its mechanism.
Enzymes are classified into six different
 groups according to the reaction being
 catalyzed. The nomenclature was
 determined by the Enzyme Commission in
 1961 (with the latest update having
 occurred in 1992), hence all enzymes are
 assigned an “EC” number. The classification
 does not take into account amino acid
 sequence (ie, homology), protein structure,
 or chemical mechanism.
   EC numbers are four digits, for example
    a.b.c.d, where “a” is the class, “b” is the
    subclass, “c” is the sub-subclass, and “d” is
    the sub-sub-subclass. The “b” and “c” digits
    describe the reaction, while the “d” digit is
    used to distinguish between different
    enzymes of the same function based on the
    actual substrate in the reaction.
   Example: for Alcohol:NAD+oxidoreductase
    EC number is 1.1.1.1
 EC   1.   Oxidoreductases
 EC   2.   Transferases
 EC   3.   Hydrolases
 EC   4.   Lyases
 EC   5.   Isomerases
 EC   6.   Ligases
 A list of the subclasses for each class is given below.
  Additional information on the sub-subclasses and sub-
  sub-subclasses (ie, full enzyme classification and
  names) can be found at the referenced web link.
 From the Web version,
  http://www.chem.qmul.ac.uk/iubmb/enzyme/index.ht
  ml
   EC 1. Oxidoreductases :catalyze the
    transfer of hydrogen or oxygen atoms or
    electrons from one substrate to another,
    also called oxidases, dehydrogenases, or
    reductases. Note that since these are
    ‘redox’ reactions, an electron
    donor/acceptor is also required to complete
    the reaction.
   EC 2. Transferases – catalyze group transfer
    reactions, excluding oxidoreductases (which
    transfer hydrogen or oxygen and are EC 1).
    These are of the general form:
   A-X + B ↔ BX + A
   EC 3. Hydrolases – catalyze hydrolytic
    reactions. Includes lipases, esterases,
    nitrilases, peptidases/proteases. These are
    of the general form:
   A-X + H2O ↔ X-OH + HA
Maltase




Maltose             Glucose   Glucose
   EC 4. Lyases – catalyze non-hydrolytic
    (covered in EC 3) removal of functional
    groups from substrates, often creating a
    double bond in the product; or the reverse
    reaction, ie, addition of function groups
    across a double bond.
   A-B     → A=B + X-Y
      X Y
    Includes decarboxylases and aldolases in
    the removal direction, and synthases in the
    addition direction.
Fumarase




Fumarate              L-malate
   EC 5. Isomerases – catalyzes isomerization
    reactions, including racemizations and cis-
    tran isomerizations.
3-phosphogycerate   2-phosphogycerate
   EC 6. Ligases -- catalyzes the synthesis of
    various (mostly C-X) bonds, coupled with
    the breakdown of energy-containing
    substrates, usually ATP
Phosphate

Pyruvate

           Oxaloacetate
a.   Cellulase
b.   L- amino acid oxidase
c.   Sucrase
d.   Maltase
e.   Succinate dehydrogenase
Group             Reaction catalyzed                      Typical reaction   Enzyme example(s) with trivial
                                                                             name
EC 1              To catalyze oxidation/reduction         AH + B → A + BH    Dehydrogenase, oxidase
Oxidoreductases   reactions; transfer of H and O atoms    (reduced)
                  or electrons from one substance to      A + O → AO
                  another                                 (oxidized)

EC 2              Transfer of a functional group from one AB + C → A + BC    Transaminase, kinase
Transferases      substance to another. The group may be
                  methyl-, acyl-, amino- or phosphate
                  group

EC 3              Formation of two products from a        AB + H2O → AOH     Lipase, amylase, peptidase
Hydrolases        substrate by hydrolysis                 + BH
EC 4              Non-hydrolytic addition or removal of   RCOCOOH →        Decarboxylase
Lyases            groups from substrates. C-C, C-N, C-O   RCOH + CO2 or
                  or C-S bonds may be cleaved             [X-A-B-Y] → [A=B
                                                          + X-Y]

EC 5              Intramolecule rearrangement,            AB → BA            Isomerase, mutase
Isomerases        i.e. isomerization changes within a
                  single molecule
EC 6              Join together two molecules by          X + Y+ ATP → XY    Synthetase
Ligases           synthesis of new C-O, C-S, C-N or C-    + ADP + Pi
                  C bonds with simultaneous breakdown
                  of ATP
A. CELLULASE catalyzes the hydrolysis
   of cellulose
B. L-AMINO ACID OXIDASE catalyses
   the oxidation of L-amino acids.
C. SUCRASE catalyses the hydrolysis of
   the disaccharide sucrose
D. MALTASE catalyses the hydrolysis of
   the disaccharide maltose
E. SUCCINATE DEHYDROGENASE
   catalyzes the removal of hydrogen
   from succinate ion
Namingandclassification

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Namingandclassification

  • 1. JESSA S. ARIÑO BSE-3B Central Bicol State University of Agriculture
  • 2.
  • 3. Enzymes are most commonly named by using a system that attempts to provide information about the function rather than the structure of the enzyme.  Type of reaction catalyzed and substrate identity are focal points for the nomenclature.  A substrate is the reactant in an enzyme- catalyzed reaction.
  • 4. 1. The suffix –ase identifies a substance as an enzyme. The suffix –in is still found in the name of the first enzymes studied such as trypsin, chymotrypsin, and pepsin. 2. The type of reaction catalyzed by an enzyme is often noted with a prefix.  oxidase- catalyzes oxidation reaction  hydrolase- catalyzes a hydrolysis reaction
  • 5. 3. The identity of the substrate is often noted in addition to the type of reaction. glucose oxidase- catalyzes oxidation of glucose lactate dehydrogenase- catalyzes the removal of hydrogen from lactate ion. Infrequently, the substrate but not the reaction type is given: Urease- catalyses the hydrolysis of urea Lactase- catalyses the hydrolysis of lactose
  • 6. According to the International union Of Biochemistry an enzyme name has two parts: -First part is the name of the substrates for the enzyme. -Second part is the type of reaction catalyzed by the enzyme. This part ends with the suffix “ase”. Example: Lactate dehydrogenase
  • 7. The International Union of Biochemistry and Molecular Biology have developed a nomenclature for enzymes, the EC numbers; each enzyme is described by a sequence of four numbers preceded by "EC". The first number classifies the enzyme based on its mechanism.
  • 8. Enzymes are classified into six different groups according to the reaction being catalyzed. The nomenclature was determined by the Enzyme Commission in 1961 (with the latest update having occurred in 1992), hence all enzymes are assigned an “EC” number. The classification does not take into account amino acid sequence (ie, homology), protein structure, or chemical mechanism.
  • 9. EC numbers are four digits, for example a.b.c.d, where “a” is the class, “b” is the subclass, “c” is the sub-subclass, and “d” is the sub-sub-subclass. The “b” and “c” digits describe the reaction, while the “d” digit is used to distinguish between different enzymes of the same function based on the actual substrate in the reaction.  Example: for Alcohol:NAD+oxidoreductase EC number is 1.1.1.1
  • 10.
  • 11.  EC 1. Oxidoreductases  EC 2. Transferases  EC 3. Hydrolases  EC 4. Lyases  EC 5. Isomerases  EC 6. Ligases  A list of the subclasses for each class is given below. Additional information on the sub-subclasses and sub- sub-subclasses (ie, full enzyme classification and names) can be found at the referenced web link.  From the Web version, http://www.chem.qmul.ac.uk/iubmb/enzyme/index.ht ml
  • 12. EC 1. Oxidoreductases :catalyze the transfer of hydrogen or oxygen atoms or electrons from one substrate to another, also called oxidases, dehydrogenases, or reductases. Note that since these are ‘redox’ reactions, an electron donor/acceptor is also required to complete the reaction.
  • 13.
  • 14. EC 2. Transferases – catalyze group transfer reactions, excluding oxidoreductases (which transfer hydrogen or oxygen and are EC 1). These are of the general form:  A-X + B ↔ BX + A
  • 15.
  • 16. EC 3. Hydrolases – catalyze hydrolytic reactions. Includes lipases, esterases, nitrilases, peptidases/proteases. These are of the general form:  A-X + H2O ↔ X-OH + HA
  • 17. Maltase Maltose Glucose Glucose
  • 18. EC 4. Lyases – catalyze non-hydrolytic (covered in EC 3) removal of functional groups from substrates, often creating a double bond in the product; or the reverse reaction, ie, addition of function groups across a double bond.  A-B → A=B + X-Y X Y  Includes decarboxylases and aldolases in the removal direction, and synthases in the addition direction.
  • 19. Fumarase Fumarate L-malate
  • 20. EC 5. Isomerases – catalyzes isomerization reactions, including racemizations and cis- tran isomerizations.
  • 21. 3-phosphogycerate 2-phosphogycerate
  • 22. EC 6. Ligases -- catalyzes the synthesis of various (mostly C-X) bonds, coupled with the breakdown of energy-containing substrates, usually ATP
  • 23. Phosphate Pyruvate Oxaloacetate
  • 24. a. Cellulase b. L- amino acid oxidase c. Sucrase d. Maltase e. Succinate dehydrogenase
  • 25. Group Reaction catalyzed Typical reaction Enzyme example(s) with trivial name EC 1 To catalyze oxidation/reduction AH + B → A + BH Dehydrogenase, oxidase Oxidoreductases reactions; transfer of H and O atoms (reduced) or electrons from one substance to A + O → AO another (oxidized) EC 2 Transfer of a functional group from one AB + C → A + BC Transaminase, kinase Transferases substance to another. The group may be methyl-, acyl-, amino- or phosphate group EC 3 Formation of two products from a AB + H2O → AOH Lipase, amylase, peptidase Hydrolases substrate by hydrolysis + BH EC 4 Non-hydrolytic addition or removal of RCOCOOH → Decarboxylase Lyases groups from substrates. C-C, C-N, C-O RCOH + CO2 or or C-S bonds may be cleaved [X-A-B-Y] → [A=B + X-Y] EC 5 Intramolecule rearrangement, AB → BA Isomerase, mutase Isomerases i.e. isomerization changes within a single molecule EC 6 Join together two molecules by X + Y+ ATP → XY Synthetase Ligases synthesis of new C-O, C-S, C-N or C- + ADP + Pi C bonds with simultaneous breakdown of ATP
  • 26. A. CELLULASE catalyzes the hydrolysis of cellulose B. L-AMINO ACID OXIDASE catalyses the oxidation of L-amino acids. C. SUCRASE catalyses the hydrolysis of the disaccharide sucrose D. MALTASE catalyses the hydrolysis of the disaccharide maltose E. SUCCINATE DEHYDROGENASE catalyzes the removal of hydrogen from succinate ion