UDP-N-乙酰葡糖胺酰基转移酶中的烃类调控因子。
Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases.
作者信息
Wyckoff T J, Lin S, Cotter R J, Dotson G D, Raetz C R
机构信息
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
出版信息
J Biol Chem. 1998 Dec 4;273(49):32369-72. doi: 10.1074/jbc.273.49.32369.
UDP-GlcNAc acyltransferase (LpxA), the first enzyme of lipid A biosynthesis, catalyzes the transfer of an acyl chain activated on acyl carrier protein (ACP) to UDP-GlcNAc. LpxAs are very selective for the lengths of their acyl donor substrates. Escherichia coli LpxA prefers R-3-hydroxymyristoyl-ACP to R-3-hydroxydecanoyl-ACP by a factor of approximately 1000, whereas Pseudomonas aeruginosa LpxA prefers the opposite. E. coli G173M LpxA and the reciprocal P. aeruginosa M169G LpxA show reversed substrate selectivity in vitro and in vivo, demonstrating the existence of precise hydrocarbon rulers in LpxAs.
UDP-N-乙酰葡糖胺酰基转移酶（LpxA）是脂多糖A生物合成的首个酶，催化酰基载体蛋白（ACP）上活化的酰基链转移至UDP-N-乙酰葡糖胺。LpxA对其酰基供体底物的长度具有高度选择性。大肠杆菌LpxA对R-3-羟基十四酰-ACP的偏好程度比对R-3-羟基癸酰-ACP高约1000倍，而铜绿假单胞菌LpxA的偏好则相反。大肠杆菌G173M LpxA和反向的铜绿假单胞菌M169G LpxA在体外和体内均表现出相反的底物选择性，证明LpxA中存在精确的烃类标尺。
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