Mitochondrial acetoacetyl-CoA thiolase deficiency is easily diagnosed by urinary organic acid analysis and can be confirmed by enzymatic analysis of cultured skin fibroblasts or blood leukocytes.
12.
The three functions are 2-enoyl coenzyme A ( CoA ) hydratase, long-chain 3-hydroxy acyl-coenzyme A dehydrogenase and long-chain 3-ketoacyl CoA thiolase.
13.
Acetoacetyl-CoA thiolase ( also called thiolase II ) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or steroid biogenesis.
14.
Acetoacetyl-CoA thiolase ( also called thiolase II ) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or steroid biogenesis.
15.
Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase ( LCHAD ), long-chain enoyl-CoA hydratase, and long-chain thiolase.
16.
Acetoacetyl-CoA thiolase ( also called thiolase II ) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyric acid synthesis or steroid biogenesis.
17.
Acetoacetyl-CoA thiolase ( also called thiolase II ) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyric acid synthesis or steroid biogenesis.
18.
It is created from acetyl-CoA by thiolase, and it is acted upon by HMG-CoA synthase to form HMG-CoA . During the metabolism of leucine, this last reaction is reversed.
19.
Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein.
20.
Members of the thiolase family can be divided into two broad categories : degradative thiolases ( EC 2.3 . 1.16 ) and biosynthetic thiolases ( EC 2.3 . 1.9 ).
