m Specific biologic proteins that catalyze

biochemical reactions without altering the

equilibrium point of the reaction or being
consumed or changed in composition

m 2 important words in the definition:

Ú ñatalyst
Ú Specific
m Onzymes speed up chemical reactions in
the body by lowering the activation
energy for the reaction to happen.
m Onzymes only catalyze certain
reactions that their active site allows
m 6s a protein : comprises a specific amino
acid sequence, with the resultant
polypeptide chains twisting, which then
folds and results in structural cavities

m Oach enzyme contains an active site as

well as an allosteric site
m 6ctive site : often a water free
cavity, this is where the
substance on which the
enzyme acts (substrate)
interacts with particular
amino acid residues
m 6llosteric site : a cavity other than the
active site which may bind
regulator molecules and
be significant only to the
basic enzyme structure
m ’soenzymes : different forms of enzyme
that may originate from
genetic or nongenetic and
maybe different from
each other based on
certain physical properties,
such as electrophoretic
mobility, solubility or
resistance to inactivation
m ’soform : results when an enzyme is
subject to posttranslational
modifications; together with
isoenzymes, contribute to the
heterogeneity in properties and
functions of enzymes
m ñofactor : a nonprotein molecule in
addition to the basic structure
of an enzyme that helps
together with enzymes that
may be necessary for enzyme
activity
m ’norganic (chloride or magnesium ions)
: ´activatorsµ
m Organic (N6 )
: ´coenzymesµ
:µprosthetic groupµ ² when
bounded tightly to an
enzyme
*apoenzyme = enzyme w/o a prosthetic
grp.
* holoenzyme = apoenzyme + prosthetic
grp.
= complete enzyme
m Onzymes are named by the Onzyme
ñommission of the ’nternational Union of
Biochemistry
m Naming is done through giving Oñ
numbers which are four digit codes
separated by a decimal.
m ëst digit ² places enzymes in one of the six
classes
m 2nd and 3rd digits ² represents the
subclass and sub-subclass of the enzyme
m 4th digit ² represents the serial number
specific to each enzyme in a sub-
subclass
ë. Oxidoreductases : catalyze a redox
reaction between two substrates
2. Transferases : catalyze the transfer
of a group other than hydrogen
from one substrate to another
3. Hydrolases : catalyze hydrolysis of
various bonds
4. Lyases : catalyze removal of groups
from substrates without hydrolysis,
product contains double bonds
5. ’somerases : catalyze the
interconversion of geometric, optical or
positional isomers
6. Ligases : catalyze the joining of two
substrate molecules, coupled with
breaking of the pyrophosphate bond in
6TP or a similar compound
m The study of the rate at which an
enzyme works is called M
M M .

Ú u

u

m Onzymes bind to their specific substrates
in the reaction to lower the activation
energy
m Onzymes exhibit saturation which occurs
when the rate becomes unresponsive to
further increases in substrate concentration.
m ’n an enzyme-catalyzed reaction:
Low substrate concentrations, rates are
proportional to substrate concentration
Higher substrate concentrations, the rate does not
increase in direct proportion
Still at higher substrate concentrations, the rate
becomes constant and unresponsive to any further
change in substrate concentration
m The previous descriptions gave the
proposal that enzyme is a two-step
process:
Ú ’nitial adsorption where the enzyme
combines with the substrate to form an
enzyme-substrate complex
Ú The enzyme-substrate complex decomposes
into the product and the free enzyme
   
m 6bsolute : enzyme combines with only
one substrate and catalyzes only the
corresponding reaction
m Group specific : enzyme combines with
all substrates containing a particular
chemical group
m Bond specific : enzymes combines with
certain substances which has a certain
bond
m Substrate concentration
> first-order kinetics = when the
reaction rate is directly proportional
to substrate concentration
> zero-order kinetics = there is an
excess free substrate and reaction
rate depends on enzyme
concentration
m Onzyme concentration
the higher the enzyme concentration
or level, the faster the reaction will
proceed since more enzymes are
present to bind with the substrate
m pH
changes in pH may denature enzymes
resulting its structural changes since
enzymes are proteins
most physiologic enzymes do about
their role at pH range of 7.0 ² 8.0
m Temperature
increasing the temperature usually
increases the rate of a chemical reaction
by increasing the movement of molecules
this is the case with enzymatic reactions
until the temperature is high enough to
denature the protein composition of the
enzyme
a ë0° increase in temperature will double
until the protein is denatured
m ’nhibitors
>competitive = binds to the active site
and compete with the substrate for the
active site
>noncompetitive = binds to sites other
than the active site and the substrate
>uncompetitive = binds to the
enzyme-substrate complex
m üixed-time
= ´end-pointµ ; enzyme is allowed to
react with the reaction and stopped at
a certain time where the measurement is
done
m ñontinuous monitoring
= ´kinetic assayµ; enzyme is made to
react with the reaction and the
measurement is done at specific time
intervals
 
 
6cid phosphatase Prostate, kidneys, RBñs, bones, spleen
6lanine aminotransferase istributed in many tissues but with high
concentrations in the liver
6lkaline phosphatase Bones, intestinal mucosa, renal tubules, liver, WBñ,
placenta
6mylase Salivary glands and pancreas
6spartate ’n almost all tissues with high concentrations in
aminotransferase cardiac and skeletal muscles

ñreatinine kinase Skeletal muscle, cardiac muscle, brain

DŽ-glutamyltransferase Tissues of the kidney, brain, prostate, pancreas, liver

Glucose-6-phosphate 6drenal complex, spleen, thymus, lymph nodes,

dehydrogenase lactating mammary gland, erythrocytes

Lactate dehydrogenase üound distributed in the body with high activities in

the heart, liver, skeletal muscle, kidney, erythrocytes
Lipase Pancreas but may also be present in the stomach
and small intestines
  

 
6cid phosphatase Prostatic carcinoma

6lanine aminotransferase Hepatic disorder

6lkaline phosphatase Hepatic disorder
Bone disorder

6mylase 6cute pancreatitis

6spartate aminotransferase 6
’

Hepatic disorder
Skeletal muscle disorder

ñreatinine kinase 6
’

Skeletal muscle disorder

DŽ-glutamyltransferase Hepatic disorder

Glucose-6-phosphate dehydrogenase rug-induced H6

Lactate dehydrogenase 6
’

Hepatic disorder
ñarcinoma

Lipase 6cute pancreatitis