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Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are protonated, resulting in a cation.
L-Arginine:glycine amidinotransferase (AGAT; EC 2.1.4.1) is the enzyme that catalyses the transfer of an amidino group from L-arginine to glycine. The products are L-ornithine and glycocyamine, also known as guanidinoacetate, the immediate precursor of creatine. Creatine and its phosphorylated form play a central role in the energy metabolism ...
Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: arginine + H 2 O → ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life.
E.g., DNA-binding proteins have their active regions rich with arginine and lysine. The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively charged amino acid, e.g., aspartate or glutamate. Leucine: L Leu
18602 Ensembl ENSG00000280908 ENSG00000159339 ENSMUSG00000025330 UniProt Q9UM07 Q9Z183 RefSeq (mRNA) NM_012387 NM_011061 RefSeq (protein) NP_036519 NP_035191 Location (UCSC) Chr 1: 17.31 – 17.36 Mb Chr 4: 140.47 – 140.5 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein-arginine deiminase type-4, is a human protein which in humans is encoded by the PADI4 gene. The protein as ...
l-Arginine l-pyroglutamate, also known as pirglutargine and arginine pidolate, is the l-arginine salt of pyroglutamic acid. Arginine pyroglutamate is a delivery form of arginine. Physical and chemical properties