EC Number   |
General Information |
Reference |
|---|
    4.1.3.4 | malfunction |
3-Hydroxy-3-methylglutaric aciduria is a rare human autosomal recessive disorder caused by deficiency of 3-hydroxy-3-methylglutaryl CoA lyase |
715807 |
| 4.1.3.4 | malfunction |
3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency is an inborn error of metabolism characterized by impairment of ketogenesis and leucine catabolism resulting in an organic acidopathy |
703092 |
| 4.1.3.4 | malfunction |
an insertion mutant strain FE6-C3 with disrupted 3-hydroxy-methylglutaryl coenzyme A lyase homologue HCL shows inability to lyse macrophages, the hcl1 mutant has a severe growth defect in bone marrow-derived macrophages. The mutant cell deficient in HMG CoA lyase accumulates acidic intermediates as a consequence of its inability to catabolize leucine, phenotype, overview |
727619 |
| 4.1.3.4 | malfunction |
inhibition of this enzyme results in reduced acetoacetate production and impaired ketoacidosis. High levels of secreted ketone bodies (acetoacetate and 3beta-hydroxybutyrate) lower the pH of blood and urine, resulting in ketoacidosis |
727117 |
| 4.1.3.4 | metabolism |
the enzyme catalyzes the last step in the leucine catabolism pathway |
727619 |
| 4.1.3.4 | physiological function |
the enzyme is a rate-limiting enzyme in hepatic cells catalyzing the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetate |
727117 |
| 4.1.3.4 | physiological function |
the enzyme is required for macrophage colonization by human fungal pathogen Histoplasma capsulatum |
727619 |
