The role of C-terminal amino acid residues of a ¦¤⁶-fatty acid desaturase from blackcurrant

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• 作者：Li-Ying Song^a ; ¹ ; ^{lysong@genetics.ac.cn} ; Wan-Xiang Lu^a ; ^b ; ¹ ; ^{wanxianglu@126.com} ; Jun Hu^a ; ^{junhu7626@yahoo.com} ; Wei-Bo Yin^a ; ^{wbyin@genetics.ac.cn} ; Yu-Hong Chen^a ; ^{yhchen@genetics.ac.cn} ; Bai-Lin Wang^c ; ^{wangbailin1@126.com} ; Richard R.-C. Wang^d ; ^{Richard.Wang@ARS.USDA.GOV} ; Zan-Min Hu^a ; ^{zmhu@genetics.ac.cn}
• 关键词：D8D ; ¦¤8-sphingolipid desaturase ; D6D ; ¦¤6-fatty acid desaturase ; LA ; linoleic acid ; ALA ; ¦Á-linolenic acid ; GLA ; ¦Ã-linolenic acid ; OTA ; octadecatetraenoic acid ; Cytb5 ; cytochrome b5 ; GC&ndash ; MS ; gas chromatography&ndash ; mass spectrometry ; aa ; amino aci
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2013
• 出版时间：22 February, 2013
• 年：2013
• 卷：431
• 期：4
• 页码：675-679
• 全文大小：423 K

文摘

¦¤⁶-fatty acid desaturase is an important enzyme in the catalytic synthesis of polyunsaturated fatty acids. Using domain swapping and a site-directed mutagenesis strategy, we found that the region of the C-terminal 67 amino acid residues of ¦¤⁶-fatty acid desaturase RnD6C from blackcurrant was essential for its catalytic activity and that seven different residues between RnD6C and RnD8A in that region were involved in the desaturase activity. Compared with RnD6C, the activity of the following mutations, V394A, K395I, F411L, S436P, VK3945AI and IS4356VP, was significantly decreased, whereas the activity of I417T was significantly increased. The amino acids N, T and Y in the last four residues also play a certain role in the desaturase activity.