Vol.1, No.4, 77-78 (2013) Advances in Enz yme Research
http://dx.doi.org/10.4236/aer.2013.14008
Letter to the Editor
Amosy E. M’Koma
School of Medicine, Meharry Medical College, Nashville, USA: amkoma@mmc.edu
Received 5 June 2013; revised 8 July 2013; accepted 23 July 2013
Copyright © 2013 Amosy E. M’Koma. This is an open access article distributed under the Creative Commons Attribution License,
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Advances in Enzyme Research (AER) is pleased to
bring you multiple new topical collections on enzyme
sciences. AER, a broad-based journal, was founded on
tenets to publish the most exciting researches with en-
zyme science advances and to encourage research, lead-
ership and application of enzymology in disease and pro-
vide a rapid turn-around time possible for reviewing and
publishing and to disseminate the articles freely for re-
search, teaching and reference purposes. As new Scien-
tific Research Open Access model, AER publishes on-
line peer-reviewed articles covering a wide range of the
advancement of science and technology in academic dis-
ciplines. The behaviors of these enzymes as biological
chemical in health and in disease, during and after medi-
cal and/or surgical interventions make AER journal a
center of academic discipline in science. Enzymes are
“biological catalysts” produced or derived from living
organism. When an enzyme is formed, it is made by
stringing together hundreds of amino acids in a very spe-
cific and unique order of chains and folds into a unique
shape that allows the enzyme to carry out specific chem-
ical reactions. An enzyme acts/speeds efficiently as a
catalyst for a specific chemical reaction. The purpose of
an enzyme in a cell is to allow the cell to carry out
chemical reactions. These reactions allow the cell to
build things or take things accordingly as needed. This is
how a cell grows and reproduces. At the most basic level,
a cell is really a little bag full of chemical reactions that
are made possible by enzymes. At any given moment, all
of the work being done inside any cell is being done by
enzymes. If you understand enzymes, then you under-
stand cells. A cell has about 1000 different types of en-
zymes floating around in the cytoplasm at any given time
waiting for the chemical they recognize to float by.
There are hundreds or millions of copies of each differ-
ent type of enzyme, depending on how important a reac-
tion is to a cell and how often the reaction is needed.
These enzymes do everything from breaking glucose
down for energy to building cell walls, constructing new
enzymes and allowing the cell to reproduce. Enzymes do
all of the work inside cells.
A good example is that you may have heard of people
who are lactose intolerant. The problem arises because
the sugar in milk, lactose, does not get broken into its
glucose components [1]. Therefore, it cannot be digested.
As the intestinal cells of individuals who are lactose in-
tolerant do not produce enough lactase, the enzyme
needed to break down lactose. This problem shows how
the lack of just one enzyme in the human body can lead
to significant problems. Sometimes there are medical
solutions to such deficiencies but many enzyme defi-
ciencies are not so easy to manage. A person who is lac-
tose intolerant can swallow a drop of lactase prior to
drinking milk or taking milk products and the problem is
solved.
Further, there are diseases that can cause enzyme defi-
ciency/malabsorption due to a number of gastrointestinal
(GI) conditions such as: in atrophic gastritis, which in-
creases with age, impairs the production of enzymes
needed to break down food and also the production of
intrinsic factor. Malabsorption would also occur with
pancreatic insufficiency [2] and of course any surgery
which removed part of e.g. the stomach [3] or small bo-
wel [4-6] would increase risk. Intestinal conditions such
as inflammatory bowel disease (Crohn’s disease (CD)
and ulcerative colitis (UC) and celiac disease (COD) can
cause significant problems. Long-term use of acid sup-
pressants such as proton pump inhibitors, H2 antagonists
is a potential risk factor, and these are some of the most
widely prescr ibed and used drugs in the eld- erly popula-
tion. Finally, in true pernicious anemia where there is an
autoimmune component, there are three dif- ferent types
of antibodies that could be the cause. Those which bind
to the intrinsic factor-vitamin B12 complex preventing
absorption, antibodies which bind to intrinsic factor itself
may prevent binding with cobalamin, and antibodies to
gastric parietal cells preventing the produc- tion of in-
trinsic factor [7]. This type of enzyme sequen- tial de-
pendence act is essential physiology to understand in
evaluating performance improvement in the treatment of
disease in clinical medicine as well as in surgical practice
as a whole. The biopatholphysiology of enzymes in dif-
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