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Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases.These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe 2+, and ascorbate.
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 group-NH 2 but is rather a secondary amine.
Pertaining to bacteria: Latin bacterium; Greek βακτήριον (baktḗrion), small staff bacteriophage, bactericide: balan-of the glans penis or glans clitoridis: Greek βάλανος (bálanos), acorn, glans balanitis: bas-of or pertaining to base Greek βάσις (básis), foundation, base basolateral bi-twice, double Latin bi-
When observed in the bacteria, Bacillus subtilis, there were potentially lethal amounts of autolysin found in the cell walls. [6] In Streptococcus pneumoniae it was found that N-acetylmuramoyl-l-alanine amidase, a cell wall autolysin, could assist in pathogenesis due to its ability to break down the wall or lyse a portion of the invading ...
Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...
The biochemical mechanism of proline racemase was first put forward in the late sixties by Cardinale and Abeles [6] using the Clostridium sticklandii enzyme, CsPRAC. The catalytic mechanism of proline racemase was late revisited by Buschiazzo, Goytia and collaborators that, in 2006, resolved the structure of the parasite TcPRAC co-crystallyzed with its known competitive inhibitor - pyrrole ...
In 2001, biologically active hydroxyproline-rich glycopeptides were isolated from tobacco which activated the production of protease inhibitors in a similar way to systemin in tomatoes. [1] Although they are structurally unrelated to systemins, their similar function resulted in them being named hydroxyproline-rich systemins (HypSys).