The Conserved Serine–Threonine–Serine Motif of the Carnitine Acyltransferases Is Involved in Carnitine Binding and Transition-State Stabilization: A Site-Directed Mutagenesis Study
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference24 articles.
1. CARNITINE
2. Specific alkylation of a histidine residue in carnitine acetyltransferase by bromoacetyl-l-carnitine
3. Some kinetic studies on the mechanism of action of carnitine acetyltransferase
4. Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a reaction-intermediate analogue
5. Catalytically important domains of rat carnitine palmitoyltransferase II as determined by site-directed mutagenesis and chemical modification. Evidence for a critical histidine residue.
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1. Evidence of a preferred kinetic pathway in the carnitine acetyltransferase reaction;Archives of Biochemistry and Biophysics;2020-09
2. CPT2 gene mutations resulting in lethal neonatal or severe infantile carnitine palmitoyltransferase II deficiency;Molecular Genetics and Metabolism;2008-08
3. Identification of 16 new disease-causing mutations in the CPT2 gene resulting in carnitine palmitoyltransferase II deficiency;Molecular Genetics and Metabolism;2006-12
4. Crystal Structures of Murine Carnitine Acetyltransferase in Ternary Complexes with Its Substrates;Journal of Biological Chemistry;2006-09
5. Crystal Structure of Mouse Carnitine Octanoyltransferase and Molecular Determinants of Substrate Selectivity*[boxs];Journal of Biological Chemistry;2005-01
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