enzyme

Enzymes are biomolecules that catalyze (i.e., increase the rates of) chemical
reactions.[1][2] Nearly all known enzymes are proteins. However, certain RNA molecules
can be effective biocatalysts too. These RNA molecules have come to be known as
ribozymes.[3] In enzymatic reactions, the molecules at the beginning of the process are
called substrates, and the enzyme converts them into different molecules, called the
products. Almost all processes in a biological cell need enzymes to occur at significant
rates. Since enzymes are selective for their substrates and speed up only a few reactions
from among many possibilities, the set of enzymes made in a cell determines which
metabolic pathways occur in that cell.

Like all catalysts, enzymes work by lowering the activation energy (Ea or ΔG‡) for a
reaction, thus dramatically increasing the rate of the reaction. Most enzyme reaction rates
are millions of times faster than those of comparable un-catalyzed reactions. As with all
catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the
equilibrium of these reactions. However, enzymes do differ from most other catalysts by
being much more specific. Enzymes are known to catalyze about 4,000 biochemical
reactions.[4] A few RNA molecules called ribozymes catalyze reactions, with an important
example being some parts of the ribosome.[5][6] Synthetic molecules called artificial
enzymes also display enzyme-like catalysis.[7]

Enzyme activity can be affected by other molecules. Inhibitors are molecules that
decrease enzyme activity; activators are molecules that increase activity. Many drugs and
poisons are enzyme inhibitors. Activity is also affected by temperature, chemical
environment (e.g., pH), and the concentration of substrate. Some enzymes are used
commercially, for example, in the synthesis of antibiotics. In addition, some household
products use enzymes to speed up biochemical reactions (e.g., enzymes in biological
washing powders break down protein or fat stains on clothes; enzymes in meat
tenderizers break down proteins, making the meat easier to chew).

The Enzyme Commission number (EC number) is a numerical classification scheme

for enzymes, based on the chemical reactions they catalyze. As a system of enzyme
nomenclature, every EC number is associated with a recommended name for the
respective enzyme.

Strictly speaking, EC numbers do not specify enzymes, but enzyme-catalyzed reactions.

If different enzymes (for instance from different organisms) catalyze the same reaction,
then they receive the same EC number. By contrast, UniProt identifiers uniquely specify
a protein by its amino acid sequence.[1]
Format of number

Every enzyme code consists of the letters "EC" followed by four numbers separated by
periods. Those numbers represent a progressively finer classification of the enzyme.

For example, the tripeptide aminopeptidases have the code "EC 3.4.11.4", whose
components indicate the following groups of enzymes:

• EC 3 enzymes are hydrolases (enzymes that use water to break up some other
molecule)
• EC 3.4 are hydrolases that act on peptide bonds
• EC 3.4.11 are those hydrolases that cleave off the amino-terminal amino acid
from a polypeptide
• EC 3.4.11.4 are those that cleave off the amino-terminal end from a tripeptide

[edit] Top level codes

Top-level EC numbers[2]
Enzyme
Typical
Group Reaction catalyzed example(s) with
reaction
trivial name
To catalyze oxidation/reduction AH + B → A +
EC 1 reactions; transfer of H and O BH (reduced) Dehydrogenase,
Oxidoreductases atoms or electrons from one A + O → AO oxidase
substance to another (oxidized)
Transfer of a functional group from
EC 2 one substance to another. The group AB + C → A + Transaminase,
Transferases may be methyl-, acyl-, amino- or BC kinase
phosphate group
EC 3 Formation of two products from a AB + H2O → Lipase, amylase,
Hydrolases substrate by hydrolysis AOH + BH peptidase
Non-hydrolytic addition or removal
EC 4 of groups from substrates. C-C, C- RCOCOOH →
Decarboxylase
Lyases N, C-O or C-S bonds may be RCOH + CO2
cleaved
Intramolecule rearrangement, i.e.
EC 5
isomerization changes within a AB → BA Isomerase, mutase
Isomerases
single molecule
Join together two molecules by
EC 6 synthesis of new C-O, C-S, C-N or X + Y+ ATP →
Synthetase
Ligases C-C bonds with simultaneous XY + ADP + Pi
breakdown of ATP
[edit] History

The enzyme nomenclature scheme was developed starting in 1955, when the
International Congress of Biochemistry in Brussels set up an Enzyme Commission.

The first version was published in 1961.

The current sixth edition, published by the International Union of Biochemistry and
Molecular Biology in 1992, contains 3196 different enzymes.

Endoenzyme
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An endoenzyme, or intracellular enzyme, is an enzyme that functions within the cell in

which it was produced. Because the majority of enzymes fall within this category, the
term is used primarily to differentiate a specific enzyme from an exoenzyme. It is
possible for a single enzyme to have both endoenzymatic and exoenzymatic functions.

Exoenzyme
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An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and that

works outside of that cell. It is usually used for breaking up large molecules that would
not be able to enter the cell otherwise. The opposite of an exoenzyme is called an
endoenzyme.

This term is also often used to refer to the hydrolytic digestive enzymes secreted by
fungi. Some extracellular enzymes: ACE: generation of angiotensin-II Lipoprotein lipase:
release of lipids from circulating lipoproteins Digestive enzymes: breakdown of ingested
nutrients Some clotting factors: e.g., thrombin