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“ENZYME SPECIFICTY”
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WHAT IS AN ENZYME?
The word "Enzyme" is derived from the Greek, en (in) +zyme (ferment).
WHAT IS A SUBSTRATE?
Active site is the region of an enzyme where substrate molecules bind and undergo
a chemical reaction. The active site consists of residues that form temporary bonds with
the substrate (binding site) and residues that catalyse a reaction of that substrate
(catalytic site). The active site is usually a groove or pocket of the enzyme which can be
located in a deep tunnel within the enzyme, or between the interfaces of multimeric
enzymes. An active site can catalyse a reaction repeatedly as its residues are not altered
at the end of the reaction (they may change during the reaction, but are regenerated by
the end).
ENZYME SPECIFICITY
TYPES OF SPECIFICITY
Enzymes vary in the specificity of the substrates that they bind to, in order to carry
out specific physiological functions. Some enzymes may need to be less specific and
therefore may bind to numerous substrates to catalyze a reaction. On the other hand,
certain physiological functions require extreme specificity of the enzyme for a single
specific substrate in order for a proper reaction and physiological phenotype to occur. The
different types of categorizations differ based on their specificity for substrates. Most
generally, they are divided into four groups: absolute, group, linkage, and stereochemical
specificity.
ABSOLUTE SPECIFICITY
GROUP SPECIFICITY
Group specificity occurs when an enzyme will only reacts with molecules that have
specific functional groups, such as aromatic structures, phosphate groups, and methyls.
One example is Pepsin, an enzyme that is crucial in digestion of foods ingested in our
diet that hydrolyzes peptide bonds in between hydrophobic amino acids, with recognition
for aromatic side chains such as phenylalanine, tryptophan, and tyrosine. Another
example is hexokinase, in enzyme involved in glycolysis that phosphorylate glucose to
produce glucose-6-phosphate. This enzyme exhibits group specificity by allowing multiple
hexoses (6 carbon sugars) as its substrate. Glucose is one of the most important
substrates in metabolic pathways involving hexokinase due to its role in glycolysis, but is
not the only substrate that hexokinase can catalyze a reaction with.
LINKAGE SPECIFICITY
STEREOCHEMICAL SPECIFICITY
The specific action of an enzyme with a single substrate can be explained using a
Lock and Key analogy first postulated in 1894 by Emil Fischer. In this analogy, the lock is
the enzyme and the key is the substrate. Only the correctly sized key (substrate) fits into
the keyhole (active site) of the lock (enzyme).
http://osp.mans.edu.eg/medbiochem_mi/Cources/Biochemistry/1st_year_medicine/Enzy
mes/files/Lecture_02.pdf
http://www.easybiologyclass.com/enzyme-substrate-specificity-types-classification/
http://biology.tutorvista.com/biomolecules/enzymes.html
http://www.worthington-biochem.com/introbiochem/specificity.html