Deficiency of 3-methylglutaconyl-coenzyme a hydratase in two siblings with 3-methylglutaconic aciduria

K. Narisawa, K. M. Gibson, L. Sweetman, W. L. Nyhan, M. Duran, S. K. Wadman

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

We studied two patients with 3-methylglutaconic aciduria in order to determine the molecular defect. A new assay for 3-methyl-glutaconyl-coenzyme A (CoA) hydratase has been developed in which the substrate, [5-14C]3-methylglutaconyl-CoA, was synthesized using 3-methylcrotonyl-CoA carboxylase purified from bovine kidney. In this assay the products of the reaction are isolated by reverse-phase high performance liquid chromatography and the rates of conversion from substrate are measured. The Michaelis constant for 3-methylglutaconyl-CoA in normal fibroblast was 6.9 μmol/liter. The mean activity of 3-methyl-glutaconyl-CoA hydratase in control fibroblasts was 495 pmol/min per mg protein. In the two patients the values were 11 and 17 pmol/min per mg protein, or 2-3% of normal.

Original languageEnglish (US)
Pages (from-to)1148-1152
Number of pages5
JournalJournal of Clinical Investigation
Volume77
Issue number4
DOIs
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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