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Only the l-arginine (symbol Arg or R) enantiomer is found naturally. [1] Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. [2] The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. [3] Like all amino acids, it is a white, water-soluble solid.
The second isozyme, Arginase II, has been implicated in the regulation of intracellular arginine/ornithine levels. It is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. It may be found at lower levels in macrophages, lactating mammary glands, and brain. [5]
This can be done in terms of the chemical elements present, or by molecular structure e.g., water, protein, fats (or lipids), hydroxyapatite (in bones), carbohydrates (such as glycogen and glucose) and DNA. In terms of tissue type, the body may be analyzed into water, fat, connective tissue, muscle, bone, etc.
In arginylation, arginine (pictured above) is added to proteins. Arginylation is a post-translational modification in which proteins are modified by the addition of arginine (Arg) at the N-terminal amino group or side chains of reactive amino acids by the enzyme, arginyltransferase (ATE1). Recent studies have also revealed that hundreds of ...
In molecular biology, an arginine finger is an amino acid residue of some enzymes. [1] [2] Arginine fingers are often found in the protein superfamily of AAA+ ATPases, GTPases, and dUTPases, where they assist in the catalysis of the gamma phosphate or gamma and beta phosphates from ATP or GTP, which creates a release of energy which can be used to perform cellular work.
Like proton NMR, carbon-13 (13 C) NMR spectroscopy is a method used in molecular structure determination. 13 C NMR reveals the types of carbons present in a molecule based on chemical shifts that correspond to certain functional groups. N-Acetylglutamic acid exhibits carbonyl carbons most distinctly due to the three carbonyl-containing ...
Argininosuccinate synthetase is a homotetramer, with each subunit consisting of 412 residues. [6] The interfaces between subunits contain a number of salt bridges and hydrogen bonds, and the C-terminus of each subunit is involved in oligomerization by interacting with the C-termini and nucleotide-binding domains of the other subunits.
The protein encoded by this gene catalyzes the penultimate step of the arginine biosynthetic pathway. There are approximately 10 to 14 copies of this gene including the pseudogenes scattered across the human genome , among which the one located on chromosome 9 appears to be the only functional gene for argininosuccinate synthetase.