Arginine: Difference between revisions
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=== Abbreviation === | === Abbreviation === | ||
Arg | [[Image:Arginine.png|right|Arginine.png]]Arg | ||
=== Single Letter Code === | === Single Letter Code === | ||
R | R | ||
=== Infomation === | === Infomation === | ||
Arginine is one of the twenty | Arginine is one of the twenty [[Amino acids|amino acids]]. It is most commonly found in its stereotypical [[L-isomer|L-isomeric formation]] and is a polar, positively charged molecule. | ||
Due to the [[Molecule|molecule's]] charge, it can sometimes be found located in the functional part of a [[Proteins|protein]] conforming a pore<ref>The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003</ref>. | Due to the [[Molecule|molecule's]] charge, it can sometimes be found located in the functional part of a [[Proteins|protein]] conforming a pore<ref>The Biology Project, Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003</ref>. | ||
Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. Its side chain contains a complex guanidinium cap on an aliphatic 3 carbon chain. Multiple [[Hydrogen bonds|H-bonds]] are able to form due to the conjugation of [[Double bond|double bonds]] and [[Lone pair|lone pairs]] on the [[Nitrogen|nitrogen]] atoms. | Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. Its side chain contains a complex guanidinium cap on an [[Aliphatic|aliphatic]] 3 [[Carbon|carbon]] chain. Multiple [[Hydrogen bonds|H-bonds]] are able to form due to the conjugation of [[Double bond|double bonds]] and [[Lone pair|lone pairs]] on the [[Nitrogen|nitrogen]] atoms. | ||
Arginine plays an important role in the last reaction of the [[Urea|urea cycle]]. In this metabolic pathway arginine is hydrolyzed by the [[Enzyme|enzyme]] [[Arginase|arginase]] in the [[Cytoplasm|cytoplasm]] to form [[Urea|urea]]<ref>Berg, J. Stryer, L. Tymoczko, J. (2011) Biochemistry, 7th Edition, New York: W.H Freeman and Company. Chapter 23, Pages 709-711</ref><ref>Berg, J. M., Tymoczko, J. L., and Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.</ref>. | |||
=== References === | === References === | ||
<references / | <references /> | ||
Latest revision as of 19:30, 16 November 2017
Abbreviation
Arg
Single Letter Code
R
Infomation
Arginine is one of the twenty amino acids. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule.
Due to the molecule's charge, it can sometimes be found located in the functional part of a protein conforming a pore[1].
Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. Its side chain contains a complex guanidinium cap on an aliphatic 3 carbon chain. Multiple H-bonds are able to form due to the conjugation of double bonds and lone pairs on the nitrogen atoms.
Arginine plays an important role in the last reaction of the urea cycle. In this metabolic pathway arginine is hydrolyzed by the enzyme arginase in the cytoplasm to form urea[2][3].
References
- ↑ The Biology Project, Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003
- ↑ Berg, J. Stryer, L. Tymoczko, J. (2011) Biochemistry, 7th Edition, New York: W.H Freeman and Company. Chapter 23, Pages 709-711
- ↑ Berg, J. M., Tymoczko, J. L., and Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.