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| '''Arginine''' (Arg) is an α-]. The L-form is one of the 20 most common natural |
'''Arginine''' (Arg) is an α-]. The L-form is one of the 20 most common natural amino acids. In mammals, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. | ||
| ==Structure== | ==Structure== | ||
| Arginine can be considered to be somewhat amphipathic amino acid as the part of the side chain nearest to the backbone is long, carbon containing and hydrophobic, whereas the end of the side chain, is a complex ] group. With p''K''<sub>a</sub> > 12, the guanidinium group is positively charged in neutral and acidic environments. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized. This group is able to form multiple ]. | |||
| ==Synthesis== | ==Synthesis== | ||
| Arginine is synthesized from citrulline by the sequential action of the cytosolic enzymes ] and ]. This is energetically costly, as the synthesis of each molecule of argininosuccinate requires hydrolysis of ] to ]; i.e., 2 ATP equivalents. Citrulline can be derived from multiple sources: from arginine via ], ] via catabolism of ] or ]/], or ADMA via DDAH. It is important to note that the pathways linking arginine, glutamine, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage. On a whole-body basis, synthesis of arginine occurs principally via the intestinal–renal axis, wherein epithelial cells of the small intestine, which produce citrulline primarily from glutamine and glutamate, collaborate with the proximal tubule cells of the kidney, which extract citrulline from the circulation and convert it to arginine, which is returned to the circulation. Consequently, impairment of small bowel or renal function can reduce endogenous arginine synthesis, thereby increasing the dietary requirement. Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that also induce ]. Thus, citrulline, a coproduct of the NOS-catalyzed reaction, can be recycled to arginine in a pathway known as the citrulline-NO or arginine-citrulline pathway. This is demonstrated by the fact that in many cell types citrulline can substitute for arginine to some degree in supporting NO synthesis. However, recycling is not quantitative because citrulline accumulates along with nitrate and nitrite, the stable end-products of NO, in NO-producing cells. | |||
| ==Function== | ==Function== | ||
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| ===In proteins=== | ===In proteins=== | ||
| The geometry, charge distribution and ability to form multiple H-bonds make |
The geometry, charge distribution and ability to form multiple H-bonds make arginine ideal for binding negatively charged groups. For this reason arginine prefers to be on the outside of the proteins where it can interact with the polar environment. | ||
| Incorporated in proteins, |
Incorporated in proteins, arginine can also be converted to ] by PAD enzymes. In addition, arginine can be ] by protein methyltransferases. | ||
| ===As a precursor=== | ===As a precursor=== | ||
| Arg is the immediate precursor of NO, urea, |
Arg is the immediate precursor of NO, urea, ornithine and agmatine; is necessary for the synthesis of ]; and can be used for the synthesis of polyamines (mainly through ornithine and to a lesser degree through agmatine), citrulline, and glutamate. | ||
| For being a precursor of NO, (relaxes blood vessels), |
For being a precursor of NO, (relaxes blood vessels), arginine is in many conditions where ] is required. | ||
| ==Sources== | ==Sources== | ||
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Arginine (Arg) is an α-amino acid. The L-form is one of the 20 most common natural amino acids. In mammals, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual.
Structure
Arginine can be considered to be somewhat amphipathic amino acid as the part of the side chain nearest to the backbone is long, carbon containing and hydrophobic, whereas the end of the side chain, is a complex guanidinium group. With pKa > 12, the guanidinium group is positively charged in neutral and acidic environments. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized. This group is able to form multiple H-bonds.
Synthesis
Arginine is synthesized from citrulline by the sequential action of the cytosolic enzymes ASS and ASL. This is energetically costly, as the synthesis of each molecule of argininosuccinate requires hydrolysis of ATP to AMP; i.e., 2 ATP equivalents. Citrulline can be derived from multiple sources: from arginine via NOS, ornithine via catabolism of proline or glutamine/glutamate, or ADMA via DDAH. It is important to note that the pathways linking arginine, glutamine, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage. On a whole-body basis, synthesis of arginine occurs principally via the intestinal–renal axis, wherein epithelial cells of the small intestine, which produce citrulline primarily from glutamine and glutamate, collaborate with the proximal tubule cells of the kidney, which extract citrulline from the circulation and convert it to arginine, which is returned to the circulation. Consequently, impairment of small bowel or renal function can reduce endogenous arginine synthesis, thereby increasing the dietary requirement. Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that also induce iNOS. Thus, citrulline, a coproduct of the NOS-catalyzed reaction, can be recycled to arginine in a pathway known as the citrulline-NO or arginine-citrulline pathway. This is demonstrated by the fact that in many cell types citrulline can substitute for arginine to some degree in supporting NO synthesis. However, recycling is not quantitative because citrulline accumulates along with nitrate and nitrite, the stable end-products of NO, in NO-producing cells. Morris SM Jr, 2004
Function
Arginine plays an important role in cell division, the healing of wounds, removing ammonia from the body, immune function, and the release of hormones.
In proteins
The geometry, charge distribution and ability to form multiple H-bonds make arginine ideal for binding negatively charged groups. For this reason arginine prefers to be on the outside of the proteins where it can interact with the polar environment. Incorporated in proteins, arginine can also be converted to citrulline by PAD enzymes. In addition, arginine can be methylated by protein methyltransferases.
As a precursor
Arg is the immediate precursor of NO, urea, ornithine and agmatine; is necessary for the synthesis of creatine; and can be used for the synthesis of polyamines (mainly through ornithine and to a lesser degree through agmatine), citrulline, and glutamate. For being a precursor of NO, (relaxes blood vessels), arginine is in many conditions where vasodilation is required.
Sources
It can be found in any protein containing foods such as meat, poultry, dairy products, fish, etc.
Reference
| Encoded (proteinogenic) amino acids | |||||||||||
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| General topics |  | ||||||||||
| By properties |
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