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大豆硬脂酰-酰基载体蛋白去饱和酶催化生成棕榈油酸酯

Palmitoleate formation by soybean stearoyl-acyl carrier protein desaturase.

作者信息

Gibson K J

机构信息

Central Research and Development Department, E.I. DuPont de Nemours, Wilmington, DE 19880-0402, USA.

出版信息

Biochim Biophys Acta. 1993 Sep 8;1169(3):231-5. doi: 10.1016/0005-2760(93)90245-5.

Abstract

Palmitoyl (hexadecanoyl)-acyl carrier protein (ACP) was found to be an alternate substrate for recombinant soybean stearoyl (octadecanoyl)-ACP delta 9-desaturase. The fatty acid product was identified as palmitoleic acid ((Z)-hexadec-9-enoic acid), which suggests that the locus of desaturation was fixed with respect to the carboxyl, not methyl, end of each substrate acyl group. The apparent specificity factor (Vmax/Km) of the desaturase for stearoyl-ACP was > 100-fold larger than for palmitoyl-ACP, mostly because of the difference in Vmax for the two substrates.

摘要

棕榈酰(十六烷酰)-酰基载体蛋白(ACP)被发现是重组大豆硬脂酰(十八烷酰)-ACP Δ9-去饱和酶的替代底物。脂肪酸产物被鉴定为棕榈油酸((Z)-十六碳-9-烯酸),这表明去饱和位点相对于每个底物酰基的羧基末端是固定的,而不是甲基末端。去饱和酶对硬脂酰-ACP的表观特异性因子(Vmax/Km)比对棕榈酰-ACP大100倍以上,这主要是由于两种底物Vmax的差异。

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