TY - JOUR
T1 - A snapshot of carnitine acetyltransferase
AU - Ramsay, Rona Ruth
AU - Naismith, James Henderson
PY - 2003/7
Y1 - 2003/7
N2 - Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.
AB - Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.
KW - TRANSITION-STATE STABILIZATION
KW - CATALYTIC MECHANISM
KW - CRYSTAL-STRUCTURE
KW - ACYLTRANSFERASES
KW - PALMITOYLTRANSFERASE
KW - ENZYMOLOGY
KW - TRANSPORT
KW - BINDING
KW - ACID
UR - http://www.scopus.com/inward/record.url?scp=0038825349&partnerID=8YFLogxK
UR - http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TCV-48Y6PR5-2&_user=1026342&_coverDate=07%2F31%2F2003&_alid=178575309&_rdoc=4&_fmt=full&_orig=search&_cdi=5180&_sort=d&_st=4&_docanchor=&_acct=C000050565&_version=1&_urlVersion=0&_userid=1026342&md5=fa6524ee502290336154a38b1d33cf8a
U2 - 10.1016/S0968-0004(03)00137-3
DO - 10.1016/S0968-0004(03)00137-3
M3 - Article
SN - 0968-0004
VL - 28
SP - 343
EP - 346
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 7
ER -