Sandbox 212
From Proteopedia
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== Substrate binding and mechanism == | == Substrate binding and mechanism == | ||
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== Regulation == | == Regulation == | ||
Revision as of 10:46, 21 December 2011
Carnitine acetyltransferase are a family of ubiquitous enzymes that play a pivotal role in cellular energy metabolism. The carnitine acetyltransferases (also known as CATs) belong to the family of enzymes known as the carnitine acyltransferases, which also includes carnitine octanoyltransferases (CrOTs) and carnitine palmityltransferase (CPTs). The three known classes of carnitine acyltransferases differ in their acyl group specificity. Carnitine acetyltransferase has a substrate preference for short chain acyl-CoAs whereas carnitine palmityltransferases and carnitine palmityltransferases show preference for long chain acyl-CoAs.They are found in the mitochondrial matrix. Carnitine acetyltransferases are localized in both the outer membrane and the inner membrane.
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Carnitine acetyltransferase
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Biological function
Overall structure of Carnitine acetyltransferase
The tertiary structure of CAT consists of 20 α-helices (α1-α20) and 16 β-strands (named β1-β16) which are arranged into two equally sized domains (N and C domains ).
