Carnitine

Carnitine (β-hydroxy-γ-N-
trimethylaminobutyric acid, 3-hydroxy-4-
N,N,N-trimethylaminobutyrate) is a
quaternary ammonium compound[1]
involved in metabolism in most mammals,
plants and some bacteria.[2] Carnitine may
exist in two isomers, labeled D-carnitine
and L-carnitine, as they are optically active.
At room temperature, pure carnitine is a
white powder, and a water-soluble
zwitterion with low toxicity. Carnitine only
exists in animals as the L-enantiomer, and
D-carnitine is toxic because it inhibits the
activity of L-carnitine.[3] Carnitine, derived
from an amino acid, is found in nearly all
organisms and animal tissue. Carnitine is
the generic expression for a number of
compounds that include L-carnitine,
acetyl-L-carnitine, and propionyl-L-
carnitine. It is most accumulated in
cardiac and skeletal muscles as it
accounts for 0.1% of its dry matter. It was
first derived from meat extracts in 1905,
therefore the name carnitine is derived
from Latin "carnus" or flesh. The body
synthesizes enough carnitine from lysine
side chains to keep up with the needs of
energy production in the body as carnitine
acts as a transporter of long-chain fatty
acids into the mitochondria to be oxidized
and produce energy. Some individuals with
genetic or medical disorders (like preterm
infants) cannot make enough, so this
makes carnitine a conditionally essential
nutrient for them.[4][5]
 Carnitine

Clinical data
AHFS/Drugs.com Micromedex Detailed
Consumer Information
Pregnancy US: B (No risk in non-
category
human studies)
Routes of Oral, intravenous
administration
ATC code A16AA01 (WHO ) (L
form)

Legal status
Legal status US: OTC

Pharmacokinetic data
 Pharmacokinetic data
Bioavailability <10%
Protein binding None
Metabolism slightly
Excretion Urine (>95%)

Identifiers

IUPAC name
3-Hydroxy-4-(trimethylazaniumyl)butanoate

CAS Number 541-15-1  

PubChem CID 288

DrugBank DB00583  

ChemSpider 282  

UNII 0G389FZZ9M
KEGG C00318  

ChEBI CHEBI:17126  

ChEMBL
 ChEMBL172513  

CompTox Dashboard DTXSID3022744

(EPA)
ECHA InfoCard 100.006.343

Chemical and physical data

Formula C7H15NO3
Molar mass 161.199 g/mol g·mol−1
3D model (JSmol) Interactive image

SMILES
C[N+](C)(C)CC(CC(=O)[O-])O

InChI
InChI=1S/C7H15NO3/c1-8(2,3)5-6(9)4-7(10)11/h6,9H,4-5H2,1-3H3 
Key:PHIQHXFUZVPYII-UHFFFAOYSA-N 

   (what is this?)  (verify)

Biosynthesis and metabolism

Many eukaryotes have the ability to
synthesize carnitine, including humans.
Humans synthesize carnitine from the
substrate TML (6-N-trimethyllysine), which
is in turn derived from the methylation of
the amino acid lysine. TML is then
hydroxylated into hydroxytrimethyllysine
(HTML) by trimethyllysine dioxygenase,
requiring the presence of ascorbic acid
and iron. HTML is then cleaved by HTML
aldolase (a pyridoxal phosphate requiring
enzyme), yielding 4-
trimethylaminobutyraldehyde (TMABA)
and glycine. TMABA is then
dehydrogenated into gamma-
butyrobetaine in an NAD+-dependent
reaction, catalyzed by TMABA
dehydrogenase. Gamma-butyrobetaine is
then hydroxylated by gamma
butyrobetaine hydroxylase (a zinc binding
enzyme) into L-carnitine, requiring iron in
the form of Fe2+.[6]

Carnitine Biosynthesis

Carnitine is involved in transporting fatty

acids across the mitochondrial membrane,
by forming a long chain acetylcarnitine
ester and being transported by carnitine
palmitoyltransferase I and carnitine
palmitoyltransferase II.[7] Carnitine also
plays a role in stabilizing Acetyl-CoA and
coenzyme A levels through the ability to
receive or give an acetyl group.[1]

Tissue distribution of
carnitine-biosynthetic enzymes

Rebouche and Engel had investigated the

tissue distribution of carnitine-biosynthetic
enzymes in humans.[8] They found TMLD
to be active in the liver, heart, muscle, brain
and highest in kidney. HTMLA activity is
found primarily in the liver. The rate of
TMABA oxidation is greatest in the liver,
with considerable activity also found in the
kidney, however is low in brain, heart and
muscle. These results indicate that all the
investigated tissues have the ability to
convert TML into butyrobetaine through
containing the required enzymes for it but
not all of them can convert butyrobetaine
into carnitine, only the kidney, liver and
brain are capable of that.[8]

Carnitine shuttle: Activation

and transportation of fatty
acids into the mitochondria
The free-floating fatty acids, released from
adipose tissues to the blood, bind to
carrier protein molecule known as serum
albumin that carry the fatty acids to the
cytoplasm of target cells such as the
heart, skeletal muscle, and other tissue
cells, where they are used for fuel. But
before the target cells can use the fatty
acids for ATP production and β oxidation,
the fatty acids with chain lengths of 14 or
more carbons must be activated and
subsequently transported into
mitochondrial matrix of the cells in three
enzymatic reactions of the carnitine
shuttle.[9]
The first reaction of the carnitine shuttle is
a two-step process catalyzed by a family
of isozymes of acyl-CoA synthetase that
are found in the outer mitochondrial
membrane, where they promote the
activation of fatty acids by forming a
thioester bond between the fatty acid
carboxyl group and the thiol group of
coenzyme A to yield a fatty acyl–CoA.[9]

In the first step of the reaction, acyl-CoA

synthetase catalyzes the transfer of
adenosine monophosphate group (AMP)
from an ATP molecule onto the fatty acid
generating a fatty acyl–adenylate
intermediate and a pyrophosphate group
(PPi). The pyrophosphate, formed from the
hydrolysis of the two high-energy bonds in
ATP, is immediately hydrolyzed to two
molecule of Pi by inorganic pyro
phosphatase. This reaction is highly
exergonic which drives the activation
reaction forward and makes it more
favorable. In the second step, the thiol
group of a cytosolic coenzyme A attacks
the acyl-adenylate, displacing AMP to form
thioester fatty acyl-CoA.[9]

In the second reaction, the activated fatty

acids that are intended for mitochondrial
oxidation are transported into the matrix
by a carrier protein, but first the acyl-CoA
must be transiently attached to the
hydroxyl group of carnitine to form fatty
acyl–carnitine. This transesterification is
catalyzed by an enzyme found in the outer
membrane of the mitochondria known as
carnitine acyltransferase 1 (also called
carnitine palmitoyltransferase 1, CPT1).[9]

The fatty acyl–carnitine ester formed then

diffuses across the intermembrane space
of the mitochondria and enters the matrix
by passive transport through the acyl-
carnitine/carnitine cotransporter that is
found in inner mitochondrial membrane.
This cotransporter return one molecule of
carnitine from the matrix to the
intermembrane space as one molecule of
fatty acyl– carnitine moves into the
matrix.[9]

In the third and final reaction of the

carnitine shuttle, the fatty acyl group is
transferred back from fatty acyl-carnitine
in the matrix to intramitochondrial
coenzyme A regenerating fatty acyl–CoA
and a free carnitine molecule. This
reaction is catalyzed by carnitine
acyltransferase 2 (also called CPT2),
which is placed on the inner face of the
inner mitochondrial membrane. The
carnitine molecule formed is then shuttled
back into the intermembrane space by the
same cotransporter while the fatty acyl-
CoA is oxidized and used for ATP
production.[9]

Regulation of fatty acid β

oxidation
The carnitine-mediated entry process is a
rate-limiting factor for fatty acid oxidation
and is an important point of regulation.[9]

Inhibition

The liver starts actively making

triglycerides from excess glucose when it
is supplied with glucose that cannot be
oxidized or stored as glycogen. This
increases the concentration of malonyl-
CoA, the first intermediate in fatty acid
synthesis, leading to the inhibition of
carnitine acyltransferase 1, thereby
preventing fatty acid entry into the
mitochondrial matrix for β oxidation. This
inhibition prevents fatty acid breakdown
while synthesis is happening.[9]

Activation

Carnitine activation occurs due to a need

for fatty acid oxidation which is required
for energy production. During vigorous
muscle contraction or during fasting, ATP
concentration decrease and AMP
concentration increase which leads to the
activation of AMP-activated protein kinase
(AMPK). AMPK phosphorylates acetyl-CoA
carboxylase which catalyzes malonyl-CoA
synthesis. This phosphorylation inhibits
the acetyl-CoA carboxylase which in turn
lowers the concentration of malonyl-CoA
and as a result it relieves the inhibition of
fatty acyl–carnitine transport into
mitochondria, thus allowing β oxidation to
replenish the supply of ATP.[9]

Transcription factors
Peroxisome proliferator-activated receptor
alpha (PPARα) is a nuclear receptor that
functions as a transcription factor. It acts
in muscle, adipose tissue, and liver to turn
on a set of genes essential for fatty acid
oxidation, including the fatty acid
transporters carnitine acyltransferases 1
and 2, the fatty acyl–CoA dehydrogenases
for short, medium, long, and very long acyl
chains, and related enzymes.[9]

PPARα functions as a transcription factor

in two cases; as mentioned before when
there is an increased demand for energy
from fat catabolism, such as during a fast
between meals or long-term starvation.
Besides that, the transition from fetal to
neonatal metabolism in the heart. In the
fetus, fuel sources in heart muscle are
glucose and lactate, but in the neonatal
heart, fatty acids are the main fuel which
require the PPARα to be activated so it is
able in turn to activate the genes essential
for fatty acid metabolism in this stage.[9]

Metabolic defects of fatty

acids oxidation
More than 20 human genetic defects in
fatty acid transport or oxidation have been
approved. In case of Fatty acid oxidation
defects, acyl-carnitines accumulate in
mitochondria and are transferred into the
cytosol, and then into the blood. Plasma
levels of acyl-carnitine in new born infants
can be detected in a small blood sample
by tandem mass spectrometry.[9]

When β oxidation is defective because of

either mutation or deficiency in carnitine,
the ω Oxidation of Fatty Acids becomes
more important in mammals. Actually, the
ω Oxidation of Fatty Acids is another
pathway for F-A degradation in some
species of vertebrates and mammals that
occurs in the endoplasmic reticulum of
liver and kidney, it is the oxidation of the ω
(omega) carbon—the carbon most far
from the carboxyl group (in contrast to
oxidation which occurs at the carboxyl end
of fatty acid, in the mitochondria).[9]

Physiological effects
Deficiency

There are two types of carnitine deficiency,

primary and secondary carnitine
deficiency. Under these circumstances
there is a specific and scientific value of
carnitine intake. Primary carnitine
deficiency is a genetic disorder of the
cellular carnitine-transporter system that
typically appears by the age of five with
symptoms of cardiomyopathy, skeletal-
muscle weakness, and hypoglycemia.
Secondary carnitine deficiencies may
happen as the result of certain disorders
such as chronic renal failure, or under
conditions that reduce carnitine
absorption or increase its excretion, for
example taking antibiotics, malnutrition,
and poor absorption.[4][10]

Supplementation

Some research has been carried out on

carnitine supplementation in athletes,
given its role in fatty acid metabolism;
however, individual responses varied
significantly in the 300 people involved in
one study.[1] Carnitine has been studied in
various cardiometabolic conditions, with a
bit of evidence pointing towards efficacy
as an adjunct in heart disease and
diabetes. However, there are insufficient
trials to determine its efficacy.[11] Carnitine
has no effect on preventing mortality
associated with cardiovascular
conditions.[12] Carnitine has no effect on
serum lipids, except a possible lowering of
LDL.[13] Carnitine has no effect on most
parameters in end stage kidney disease,
however it possibly has an effect on c-
reactive protein. The effects on mortality
and disease outcome are unknown.[14]
Male infertility

The carnitine content of seminal fluid is

directly related to sperm count and
motility, suggesting that the compound
might be of value in treating male
infertility. One study concluded that
carnitine supplementation may improve
sperm quality, and the reported benefits
may relate to increased mitochondrial
fatty-acid oxidation (providing more energy
for sperm) and reduced cell death in the
testes of mice subjected to physical stress
to the testes.[15]

Cardiovascular and peripheral

arterial diseases

Several studies have approved the

effectiveness of supplemental carnitine in
the management of cardiac ischemia
(restriction of blood flow to the heart) and
peripheral arterial disease. In fact, levels of
carnitine are low in the failing heart
muscle, supplemental amounts might
counteract the toxic effects of free fatty
acids and improve carbohydrate
metabolism. Carnitine has had anti-
ischemic properties when given orally and
by injection.[16][17]

Atherosclerosis
An important interaction between diet and
the intestinal microbiome brings into play
additional metabolic factors that
aggravate atherosclerosis beyond dietary
cholesterol. This may help to explain some
benefits of the Mediterranean diet. Work
by Robert Koeth et al., from the Cleveland
Clinic reported that carnitine[18] from
animal flesh (four times as much in red
meat as in fish or chicken), as well as
phosphatidylcholine from egg yolk, are
converted by intestinal bacteria to
trimethylamine (the compound that
causes uremic breath to smell fishy).
Trimethylamine is oxidized in the liver to
trimethylamine N-oxide (TMAO), which
causes atherosclerosis in animal models.
Patients in the top quartile of TMAO had a
2.5-fold increase in the 3-year risk of
stroke, death, or myocardial infarction.

A key issue is that vegans who consumed

L-carnitine did not produce TMAO because
they did not have the intestinal bacteria
that produce TMA from carnitine.[19]

Diabetes mellitus type 2

Type 2 diabetes which is marked by insulin

resistance may be associated with a
defect in fatty acid oxidation in muscle.
Several studies suggest that carnitine
supplementation may have a beneficial
effect on glucose utilization and reduce
diabetic neuropathy. However carnitine
may also increase overall cardio-metabolic
risk.[20]

AIDS and HIV

Generally HIV infected patients

accumulate fat in some areas of the body
and lose fat in other areas, besides having
high blood levels of fats (hyperlipidemia)
and insulin resistance which is known as
the lipdystrophy syndrome. This syndrome
causes a deficiency in L-carnitine which
causes defects in fat metabolism in
mitochondria.[21] Supplementation with
carnitine in HIV-infected individuals may
slow the death of lymphocytes, reduce
neuropathy and favorably affect blood lipid
levels.[21]

Hemodialysis

End stage renal disease and

Hemodialysis
The kidneys contribute to overall
homeostasis in the body, including
carnitine levels. In the case of renal
impairment, urinary elimination of
carnitine increasing, endogenous
synthesis decreasing, and poor nutrition
as a result of disease-induced anorexia
can result in carnitine deficiency. Carnitine
blood levels and muscle stores can
become very low, which may contribute to
anemia, muscle weakness, fatigue, altered
levels of blood fats, and heart disorders.
Some studies have shown that
supplementation of high doses of L-
carnitine (often injected) may aid in
anemia management.[22][23]
Sources
Carnitine is a chiral molecule, meaning
that it exists as two isomers (L-carnitine
and D-carnitine), each of which is a mirror
image of the other. The form present in the
body is L-carnitine, which is also the form
present in food. Food sources rich in L-
carnitine are animal products such as
meat, poultry, fish, and milk. Redder meats
tend to have higher levels of L-
carnitine.[4][13][24] Adults eating diverse
diets that contain animal products attain
about 60–180 milligrams of carnitine per
day.[25] Vegans get noticeably less (about
10–12 milligrams) since their diets lack
these carnitine-rich animal-derived foods.
Approximately 54% to 86% of dietary
carnitine is absorbed in the small intestine
and then enters the bloodstream.[25][4]
Even carnitine-poor diets have little effect
on the body’s total carnitine content as the
kidneys conserve carnitine very
efficiently.[4][13] The carnitine content of
several foods is listed in Table 1.

Table 1: Selected food sources of carnitine

Food Milligrams (mg)

Beef steak, cooked, 4 ounces 56–162

Ground beef, cooked, 4 ounces 87–99

Milk, whole, 1 cup 8

Codfish, cooked, 4 ounces 4–7

Chicken breast, cooked, 4 ounces 3–5

Ice cream, ½ cup 3

Cheese, cheddar, 2 ounces 2

Whole–wheat bread, 2 slices 0.2

Asparagus, cooked, ½ cup 0.1

In general omnivorous humans consume
2–12 µmol of carnitine per day per kg of
body weight that forms 75% of body
carnitine. Humans produce 1.2 µmol per
day per kg of body weight of carnitine
endogenously which is 25% of body
carnitine.[26][27][28] Strict vegetarians obtain
very little of carnitine from diet (0.1 µmol
per day per kg of body weight) as carnitine
is mainly found in foods coming from
animals. This means that 90% of their
body carnitine is obtained through
biosynthesis.[27] However this difference
of plasma levels of carnitine between
omnivorous humans and strict vegetarians
is possibly not of any clinical
significance.[29][30]

Recommended intakes of
carnitine

In 1989, the Food and Nutrition Board

(FNB) concluded that carnitine wasn't an
essential nutrient as healthy human liver
and kidneys synthesize sufficient
quantities of carnitine from lysine and
methionine to meet up with daily body
requirements without the need of
consuming it from supplements or
food.[24][4] Also, the FNB has not
established Dietary Reference Intakes
(DRIs) for carnitine.[31]

Supplemental sources of
carnitine

L-carnitine, acetyl-L-carnitine, and

propionyl-L-carnitine are available in
nutraceutical dietary supplement pills or
powders. It is also a drug approved by the
Food and Drug Administration to treat
primary and certain secondary carnitine-
deficiency syndromes.[5]

Carnitine and medication

interactions
1. Carnitine interacts with pivalate-
conjugated antibiotics such as
pivampicillin. Chronic administration of
these antibiotics increases the excretion
of pivaloyl-carnitine, which can lead to
carnitine depletion.[4][25]

2. Treatment with the anticonvulsants

valproic acid, phenobarbital, phenytoin, or
carbamazepine significantly reduces
blood levels of carnitine. In addition, the
use of valproic acid may cause
hepatotoxicity. (L-carnitine administration
may help treat valproic acid toxicity in
children and adults)[32][33]
History
Levocarnitine was approved by the U.S.
Food and Drug Administration as a new
molecular entity under the brand name
Carnitor on December 27, 1985.[34]

See also
Acetylcarnitine
Gamma-butyrobetaine dioxygenase
Glycine Propionyl-L-Carnitine (GPLC)
Meldonium
Systemic primary carnitine deficiency

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31. Institute of Medicine. Food and
Nutrition Board. Dietary Reference
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http://www.iom.edu/project.asp?
id=4574.
32. Hug G, McGraw CA, Bates SR,
Landrigan EA (November 1991).
"Reduction of serum carnitine
concentrations during anticonvulsant
therapy with phenobarbital, valproic
acid, phenytoin, and carbamazepine in
 children". The Journal of Pediatrics.
119 (5): 799–802. PMID 1941389 .
33. Lheureux PE, Hantson P (February
2009). "Carnitine in the treatment of
valproic acid-induced toxicity". Clinical
Toxicology. 47 (2): 101–11.
doi:10.1080/15563650902752376 .
PMID 19280426 .
34. FDA approval letter

Further reading
Stanley, Charles A.; Bennett, Michael J.;
Longo, Nicolo (2000). "Plasma Membrane
Carnitine Transport Defect". In Scriver, C.W.;
Beaudet, A.L.; Sly, W.S.; Valle, D. (eds.).
Metabolic and Molecular Bases of Inherited
Disease (8th ed.). New York, NY, USA:
McGraw Hill. doi:10.1036/ommbid.297 .
ISBN 978-0-07-913035-8. Retrieved
22 January 2016.
Steiber A, Kerner J, Hoppel CL (2004).
"Carnitine: a nutritional, biosynthetic, and
functional perspective". Molecular Aspects of
Medicine. 25 (5–6): 455–73.
doi:10.1016/j.mam.2004.06.006 .
PMID 15363636 .
Marcovina SM, Sirtori C, Peracino A,
Gheorghiade M, Borum P, Remuzzi G,
Ardehali H (February 2013). "Translating the
basic knowledge of mitochondrial functions
to metabolic therapy: role of L-carnitine" .
Translational Research. 161 (2): 73–84.
doi:10.1016/j.trsl.2012.10.006 .
PMC 3590819 . PMID 23138103 .
Johri AM, Heyland DK, Hétu MF, Crawford B &
Spence JD (August 2014). "Carnitine therapy
for the treatment of metabolic syndrome and
cardiovascular disease: evidence and
controversies" (print, online review). Nutrition,
Metabolism, and Cardiovascular Diseases. 24
(8): 808–14.
doi:10.1016/j.numecd.2014.03.007 .
PMID 24837277 . Retrieved 22 January
2016.
Dambrova M, Liepinsh E (February 2015).
"Risks and benefits of carnitine
supplementation in diabetes". Experimental
and Clinical Endocrinology & Diabetes. 123
 (2): 95–100. doi:10.1055/s-0034-1390481 .
PMID 25343268 .
Brown JM, Hazen SL (2015). "The gut
microbial endocrine organ: bacterially
derived signals driving cardiometabolic
diseases" . Annual Review of Medicine. 66:
343–59. doi:10.1146/annurev-med-060513-
093205 . PMC 4456003 . PMID 25587655 .

External links
National Institutes of Health fact sheet
on carnitine
Molecule of the Month at University of
Bristol
Retrieved from
"https://en.wikipedia.org/w/index.php?
title=Carnitine&oldid=893519841"

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