G LY C IN E

Glycine is one of the non-essential amino acids and is used to help

create muscle tissue and convert glucose into energy. It is also
essential to maintaining healthy central nervous and digestive
systems, and has recently been shown to provide protection via
antioxidants from some types of cancer.

Glycine is used in the body to help construct normal DNA and RNA
strands—the genetic material needed for proper cellular function and
formation. It helps prevent the breakdown of muscle by boosting the
body’s levels of creatine, a compound that helps build muscle mass.
High concentrations of glycine are found not only in the muscles, but
in the skin and other connective tissues as well. Almost 1/3 of
collagen, which keeps the skin and connective tissue firm and flexible,
is composed of glycine. (High amounts of Glycine are also found in
gelatin, which is a form of denatured collagen). Without glycine the
body would not be able to repair damaged tissues; the skin would
become slack as it succumbed to UV rays, oxidation, and free radical
damage, and wounds would never heal.

Glycine is considered a glucogenic amino acid, which means it helps

supply the body with glucose needed for energy. It helps regulate
blood sugar levels, and thus glycine supplementation may be useful for
treating symptoms characterized by low energy and fatigue, such as
hypoglycemia, anemia, and Chronic Fatigue Syndrome (CFS).

Glycine is essential for a healthy, normally functioning digestive

system. It helps regulate the synthesis of the bile acid used to digest
fats, and is included in many commercial gastric antacid agents.

Glycine is necessary for central nervous system function. Research has

shown that this amino acid can help inhibit the neurotransmitters that
cause seizure activity, hyperactivity, and manic (bipolar) depression.
Glycine can also be converted to another neurotransmitter, serine, as
needed, and may be beneficial in the management of schizophrenia. In
one study, twenty-two schizophrenic patients, who did not initially
respond to traditional treatments, added glycine to their ongoing
antipsychotic medication and found that it significantly reduced their
symptoms. Glycine intake among the participants ranged from 40 to
90 grams daily (0.8 grams per kilogram of body weight). More
research concerning the effects of glycine on schizophrenia is
underway. Studies have shown that glycine also helps improve
memory retrieval loss in those that suffer from a wide variety of sleep-
depriving conditions, including schizophrenia, Parkinson’s disease,
Huntington’s disease, jet lag, and overwork.

Results from preliminary studies of glycine as a potential treatment for

cancer have been promising, and suggest that it may help prevent the
development of cancerous tumors and melanoma. In laboratory mice,
dietary glycine prevented tumor growth by inhibiting angiogenisis, the
process by which tumors develop their own blood supply. Glycine also
seems to play a role in keeping the prostate healthy. In one study,
glycine was shown to help reduce the symptoms of prostatic
hyperplasia in men.

High-protein foods, such as fish, meat, beans, milk, and cheese, are
the best dietary sources of glycine. Glycine is also available in capsule
and powder forms, and as part of many combination amino acid
supplements. There have been no toxic effects associated with glycine,
although some people have reported that taking this supplement
causes stomach upset.

Individuals with kidney or liver disease should not consume glycine

without consulting their doctor. Taking any one amino acid supplement
can cause a disruption of the citric acid or Krebs cycle, and cause a
build-up of nitrogen or ammonia in the body, which makes the liver
and kidneys work harder to remove waste. Anyone taking antispastic
drugs should consult a physician before supplementing with glycine,
since it theoretically could increase the effects of these medications

A LA N I N E

Alanine, or L-alanine, is an amino acid that helps the body convert the
simple sugar glucose into energy and eliminate excess toxins from the
liver. Amino acids are the building blocks of protein, and are key to
building strong, healthy muscles—alanine has been shown to help
protect cells from being damaged during intense aerobic activity, when
the body cannibalizes muscle protein to help produce energy.

Alanine is crucial for preserving balanced levels of nitrogen and

glucose in the body, which it does through a series of chemical actions
called the alanine cycle. During the alanine cycle, any excess amino
acids (proteins) in cells or tissues are transferred to a receptor
molecule called pyruvate, which is produced by the breakdown of
glucose. The pyruvate is then converted to alanine and transferred to
the liver. The liver extracts nitrogen from alanine and converts some
of it back into pyruvate, which can then be used to produce more
glucose. Any excess nitrogen is then converted into urea and passed
out of the body during urination. This cycle, glucose—pyruvate—
alanine—pyruvate—glucose, helps supply the body with the energy it
needs to support cellular life. It also ensures that a constant supply of
pyruvate is available to allow the synthesis of glucose and amino acids
in the body.

Alanine plays a key role in maintaining glucose levels and thus energy
supplies in the body. Epstein-Barr virus and chronic fatigue syndrome
have been linked to excessive alanine levels and low levels of tyrosine
and phenylalanine. Alanine may help regulate blood sugar as well.
Research has found that for people with insulin-dependent diabetes,
taking an oral dose of L-alanine effectively prevents nighttime
hypoglycemia.

Alanine is a nonessential amino acid, which means that a healthy body

is able to manufacture its own supply of this substance. However, all
amino acids may become essential (requiring dietary supplementation)
if the body is for some reason unable to produce them. People with
low-protein diets or eating disorders, liver disease, diabetes, or genetic
conditions that cause Urea Cycle Disorders (UCDs), may need to take
alanine supplements to avoid a deficiency. Low levels of alanine have
been found in patients with hypoglycemia, diabetes, and hepatitis—it
is not known at this time if alanine deficiency is the cause or result of
these diseases. The body must have alanine to process the B vitamins
so necessary for good health, especially vitamin B5 (pantothenic acid)
and vitamin B6 (pyridoxine).

Because fluid in the prostate gland contains alanine, it has been

theorized that this amino acid may help treat benign prostatic
hyperplasia (BPH), a condition in which the prostate becomes enlarged
and causes urination discomfort. In one study, participants with BPH
took 780 milligrams of alanine, glycine, and glutamic acid per day for
two weeks, then 390 milligrams of these three amino acids for the
next two and a half months, and saw a significant reduction in
symptoms.

Good sources of alanine are meat, poultry, eggs, dairy products, and
fish. Some protein-rich plant foods like avocado also supply alanine.
There are also a number of supplements containing alanine available
on the market. However, keep in mind that taking any one amino acid
could upset the balance of nitrogen in the body, and make it harder for
the liver and kidneys eliminate waste. People with liver or kidney
disease should consult a physician before taking any amino acid
supplement.

A LA N I N E

From Wikipedia, the free encyclopedia

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Alanine

IUPAC name
[show]

Identifiers

CAS number [56-41-7]

PubChem 5950

SMILES [show]

Properties

Molecular formula C3H7NO2

Molar mass 89.09 g mol−1

Supplementary data page

Structure and
n, εr, etc.
properties

Thermodynamic Phase behaviour

data Solid, liquid, gas

Spectral data UV, IR, NMR, MS

 Except where noted otherwise, data are given
for
materials in their standard state
(at 25 °C, 100 kPa)
Infobox references

Alanine (abbreviated as Ala or A)[1] is an α-amino acid with the chemical formula
CH3CH(NH2)COOH. The L-isomer is one of the 20 proteinogenic amino acids, i.e. the
building blocks of proteins. Its codons are GCU, GCC, GCA, and GCG. It is classified as
a nonpolar amino acid. L-alanine is second only to leucine, accounting for 7.8% of the
primary structure in a sample of 1,150 proteins.[2] D-alanine occurs in bacterial cell walls
and in some peptide antibiotics.

Contents
[hide]

• 1 Structure
• 2 Sources
o 2.1 Dietary Sources
o 2.2 Biosynthesis
o 2.3 Chemical Synthesis
• 3 Physiological function
o 3.1 As a carrier of ammonia and of the carbon skeleton of pyruvate in
alanine cycle
o 3.2 Link to hypertension
• 4 Chemical properties
o 4.1 Free radical stability
• 5 References

• 6 See also

[edit] Structure

The α-carbon atom of alanine is bound with a methyl group (-CH3), making it one of the
simplest α-amino acids with respect to molecular structure and also resulting in alanine
being classified as an aliphatic amino acid. The methyl group of alanine is non-reactive
and is thus almost never directly involved in protein function.

(S)-Alanine (left) and (R)-alanine (right) in zwitterionic form at neutral pH

A high potency artificial sweetener, called suosan, is derived from beta-alanine[3].

[edit] Sources
[edit] Dietary Sources

Alanine is a nonessential amino acid, meaning it can be manufactured by the human

body, and does not need to be obtained directly through the diet. Alanine is found in a
wide variety of foods, but is particularly concentrated in meats.

Good sources of alanine include:

• Animal sources: meat, seafood, caseinate, dairy products, eggs, fish, gelatin,
lactalbumin
• Vegetarian sources: beans, nuts, seeds, soy, whey, brewer's yeast, brown rice
bran, corn, legumes, whole grains.

[edit] Biosynthesis

Alanine can be manufactured in the body from pyruvate and branched chain amino acids
such as valine, leucine, and isoleucine.

Alanine is most commonly produced by reductive amination of pyruvate. Because

transamination reactions are readily reversible and pyruvate pervasive, alanine can be
easily formed and thus has close links to metabolic pathways such as glycolysis,
gluconeogenesis, and the citric acid cycle. It also arises together with lactate and
generates glucose from protein via the alanine cycle.

[edit] Chemical Synthesis

Racemic alanine can be prepared via the condensation of acetaldehyde with ammonium
chloride in the presence of potassium cyanide by the Strecker reaction.[4]

[edit] Physiological function

[edit] As a carrier of ammonia and of the carbon skeleton of pyruvate
in alanine cycle

Alanine plays a key role in glucose-alanine cycle between tissues and liver. In muscle
and other tissues that degrade amino acids for fuel, amino groups are collected in the
form of glutamate by transamination. Glutamate can then transfer its amino group
through the action of alanine aminotransferase to pyruvate, a product of muscle
glycolysis, forming alanine and alpha-ketoglutarate. The alanine formed is passed into
the blood and transported to the liver. A reverse of the alanine aminotransferase reaction
takes place in liver. Pyruvate regenerated forms glucose through gluconeogenesis, which
returns to muscle through the circulation system. Glutamate in the liver enters
mitochondria and degrades into ammonium ion through the action of glutamate
dehydrogenase, which in turn participate in the urea cycle to form urea.[5]
The glucose-alanine cycle enables pyruvate and glutamate to be removed from the
muscle and find their way to the liver. Glucose is regenerated from pyruvate and then
returned to muscle: the energetic burden of gluconeogenesis is thus imposed on the liver
instead of the muscle. All available ATP in muscle is devoted to muscle contraction.[5]

[edit] Link to hypertension

An international study led by Imperial College London found a correlation between high
levels of alanine and higher blood pressure, energy intake, cholesterol levels, and body
mass index.[6]

[edit] Chemical properties

[edit] Free radical stability

The deamination of an alanine molecule produces a stable alkyl free radical,

CH3C•HCOO–. Deamination can be induced in solid or aqueous alanine by radiation.[7]

This property of alanine is used in dosimetric measurements in radiotherapy. When

normal alanine is irradiated, the radiation causes certain alanine molecules to become free
radicals, and, as these radicals are stable, the free radical content[citation needed] can later be
measured in order to find out how much radiation the alanine was exposed to. In this
way, one can be assured that complex radiotherapy treatment plans will deliver the
intended pattern of radiation dose.