Molecular cloning and expression of fatty acid alpha-hydroxylase from Sphingomonas paucimobilis
Molecular cloning and expression of fatty acid alpha-hydroxylase from Sphingomonas paucimobilis
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DOI：
10.1074/jbc.272.38.23592
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发表时间：
1997-09-19
影响因子：
4.8
通讯作者：
Ichihara, K
中科院分区：
文献类型：
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作者：
Matsunaga, I;Yokotani, N;Ichihara, K
脂肪酸α-羟化酶（FAAH）催化脂肪酸α-氧化生成2-羟基脂肪酸的起始反应，在从原核生物到真核生物的许多生物中都检测到了FAAH活性。从少动鞘氨醇单胞菌（Sphingomonaspaucimobilis）中克隆了FAAH基因，该基因编码415个氨基酸。同源性分析表明，FAAH中存在细胞色素P450（P450）高度保守的氨基酸序列。血红素结合区的共有序列通过插入而被修饰。总的来说，FAAH与已知的P450没有明显的同源性，重组FAAH的CO差光谱显示出P450的特征性光谱，除了该峰位于445 nm处。这些结果表明细菌FAAH是P450超家族的新成员。
Fatty acid alpha-hydroxylase (FAAH) catalyzes the initial reaction in alpha-oxidation of fatty acid to produce 2-hydroxy fatty acid, FAAH activity has been detected in a wide range of organisms from prokaryotes to eukaryotes. Here, we describe cloning of the FAAH gene from Sphingomonas paucimobilis, a sphingolipid- and 2-hydroxyristic acid-rich bacterium, The isolated gene encoded 415 amino acids, A homology search revealed that amino acid sequences highly conserved in cytochrome P450 (P450) were present in FAAH, Although the heme-bindimg cysteine was recognizable at position 361, the consensus in the heme-binding region was modified by an insertion. Overall, FAAH has no significant identity to the known P450s, CO difference spectrum of recombinant FAAH showed the characteristic one of P450, except this peak was at 445 nm. These results suggest bacterial FAAH is a novel member of the P450 superfamily.