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The most obvious, first effects (gingival and hair problems) of absence of ascorbic acid in humans come from the resulting defect in hydroxylation of proline residues of collagen, with reduced stability of the collagen molecule, causing scurvy. Increased serum and urine levels of hydroxyproline have also been demonstrated in Paget's disease. [10]
Procollagen-proline dioxygenase catalyzes the following reaction: L-proline + alpha-ketoglutaric acid + O 2 → (2S, 4R)-4-hydroxyproline + succinate + CO 2. The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: [3] In the first, a highly reactive Fe(IV)=O species is produced.
Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene. [5] [6] This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the ...
The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase. Other names in common use include Skp1-HyPro GlcNAc-transferase , UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide , GlcNAc-transferase , UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase , and UDP ...
Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate".
The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase. Other names in common use include hydroxyproline epimerase , hydroxyproline 2-epimerase , and L-hydroxyproline epimerase . This enzyme participates in arginine and proline metabolism .
The mutation in the gene encodes prolyl 3-hydroxylase 1. The malfunctioning prolyl 3-hydroxylase in leprecan leads to inappropriate collagen folding. This is due to the instability caused by the absence of hydroxyproline. Hydroxyproline is the product of hydroxylating a proline residue. [5]
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).