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Proline (symbol Pro or P) [4] is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino ...
In enzymology, a proline—tRNA ligase (EC 6.1.1.15) is an enzyme that catalyzes the chemical reaction. ATP + L-proline + tRNAPro AMP + diphosphate + L-prolyl-tRNAPro. The 3 substrates of this enzyme are ATP, L-proline, and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro).
The adenylation activity is catalyzed by the bifunctional adenylyltransferase/adenylyl removal (AT/AR) enzyme. Glutamine and a regulatory protein called PII act together to stimulate adenylation. [3] This diagram shows the biosynthesis (anabolism) of amino acids glutamate, glutamine, proline, and arginine from the precursor alpha-ketoglutarate.
The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. [ 6 ] Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple ...
Arginine and proline metabolism is one of the central pathways for the biosynthesis of the amino acids arginine and proline from glutamate. The pathways linking arginine, glutamate, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage.
In proline degradation, the enzyme proline dehydrogenase produces P5C from proline, and the enzyme 1-pyrroline-5-carboxylate dehydrogenase converts GSA to glutamate. In many prokaryotes, proline dehydrogenase and P5C dehydrogenase form a bifunctional enzyme that prevents the release of P5C during proline degradation. [9]
Proline and its higher homolog pipecolic acid affect the secondary structure of protein. D-alpha-amino acid - L-alpha-amino acid sequence can induce beta hairpin. [1] It suggested that acyclic secondary amino acids are more flexible than cyclic secondary amino acids in protein by replacement of pipecolic acid by N-methyl-L-alanine in efrapeptin C.
Delta-1-pyrroline-5-carboxylate synthetase (P5CS) is an enzyme that in humans is encoded by the ALDH18A1 gene. [5] [6] This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities.