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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.
Some cells synthesize argininosuccinic acid from citrulline and aspartic acid and use it as a precursor for arginine in the urea cycle (or citrulline-NO cycle), releasing fumarate as a by-product to enter the TCA cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. [3] [4]
The systematic name of this enzyme class is N2-succinyl-L-arginine iminohydrolase (decarboxylating). Other names in common use include N2-succinylarginine dihydrolase, arginine succinylhydrolase, SADH, AruB, AstB, and 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). This enzyme participates in arginine and proline metabolism.
Arginine alpha-ketoglutarate (AAKG) is a salt of the amino acid arginine and alpha-ketoglutaric acid. It is marketed as a bodybuilding supplement. [1] Peer-reviewed studies have found no increase in muscle protein synthesis or improvement in muscle strength from use of AAKG as a dietary supplement. [1] [2] [3]
The enzyme Acid-Induced Arginine Decarboxylase (AdiA) (EC 4.1.1.19), also commonly referred to as arginine decarboxylase, catalyzes the conversion of L-arginine into agmatine and carbon dioxide. The process consumes a proton in the decarboxylation and employs a pyridoxal-5'-phosphate (PLP) cofactor , similar to other enzymes involved in amino ...
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.
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