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X-Pro Dipeptidase
Xaa-Pro dipeptidase (, '' prolidase'', ''imidodipeptidase'', ''proline dipeptidase'', ''peptidase D'', ''gamma-peptidase'') is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of Xaa!Pro dipeptides; also acts on aminoacyl-hydroxyproline (2''S'',4''R'')-4-Hydroxyproline, or L-hydroxyproline ( C5 H9 O3 N), is an amino acid, abbreviated as Hyp or O, ''e.g.'', in Protein Data Bank. Structure and discovery In 1902, Hermann Emil Fischer isolated hydroxyproline from hydrolyzed gela ... analogs This enzyme is Mn2+-activated. References External links * {{Portal bar, Biology, border=no EC 3.4.13 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prolidase
Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the ''PEPD'' gene. Prolidase is an enzyme in humans that plays a crucial role in protein metabolism and collagen recycling through the catalysis of the rate-limiting step in these chemical reactions. This enzyme is coded by the gene PEPD (peptidase D), located on chromosome 19. Serum prolidase activity is also currently being explored as a biomarker for diseases. Function Xaa-Pro dipeptidase is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus (but not Pro-Pro). It is important in collagen metabolism because of the high levels of imino acids. Mutations at the PEPD locus cause prolidase deficiency. This is characterised by Iminodipeptidurea, skin ulcers, mental retardation and recurrent infections. Serum prolidase falls into the category of proteases, specifically exopeptidases. These EC numbers range from 3.4.11 to 3.4.19. Structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
