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Substrate specificity of manganese-activated prolidase in control and prolidase-deficient cultured skin fibroblasts.

Abstract
Skin fibroblasts have a single enzyme, Mn2+-activated prolidase, that hydrolyses a range of amino acid-proline dipeptides. Two cases of prolidase deficiency showed a marked loss of activity against glycyl-proline irrespective of Mn2+ conditions. However, the abnormal enzyme showed only moderate reductions in activity against phenylalanyl-, alanyl-, and leucyl-proline following preincubation with Mn2+ or addition of Mn2+ with the substrate. Control prolidase was stable to prolonged preincubation with Mn2+, whereas the abnormal prolidase was progressively inactivated. The findings indicate, for at least the present two cases, that prolidase deficiency results from an altered rather than a marked reduction in the amount of normal enzyme.
AuthorsJ Butterworth, D Priestman
JournalJournal of inherited metabolic disease (J Inherit Metab Dis) Vol. 7 Issue 1 Pg. 32-4 ( 1984) ISSN: 0141-8955 [Print] ENGLAND
PMID6429439 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Manganese
  • Proline
  • Dipeptidases
  • proline dipeptidase
Topics
  • Amino Acid Metabolism, Inborn Errors (enzymology)
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Dipeptidases (deficiency)
  • Fibroblasts (enzymology)
  • Humans
  • Male
  • Manganese (metabolism)
  • Proline (metabolism)
  • Skin (enzymology)
  • Substrate Specificity

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