不动杆菌属HO1-N的外膜磷脂酶A
Outer membrane phospholipase A from Acinetobacter sp. HO1-N.
作者信息
Torregrossa R E, Makula R A, Finnerty W R
出版信息
J Bacteriol. 1977 Aug;131(2):493-8. doi: 10.1128/jb.131.2.493-498.1977.
A phospholipase A1 activity that hydrolyzed cardiolipin to triacyl- and diacyl-lysocardiolipin was localized in outer membrane preparations derived from Acinetobacter sp. HO1-N. The specific activity of the enzyme derived from hexadecane-grown cells was 2.5 to 3 times higher than that derived from NBYE-grown cells. An apparent Km of 2.22 mM was determined, although inhibition kinetics resulted at the higher cardiolipin substrate concentrations. Optimal reaction conditions established on metal requirements. Enzyme activity was obligately dependent on Triton X-100 (0.5%) and was inhibited by cationic and anionic detergents. Cardiolipin-specific phospholipase D converted triacyl-lysocardiolipin to lysophosphatidylglycerol and phosphatidic acid. The specific activity of this enzyme was approximately 100 times greater than that reported for other membrane preparations derived from microorganisms.
一种能将心磷脂水解为三酰基和二酰基溶血心磷脂的磷脂酶A1活性定位于源自不动杆菌属HO1-N的外膜制剂中。十六烷培养的细胞所产生的该酶的比活性比NBYE培养的细胞所产生的酶高2.5至3倍。尽管在较高的心磷脂底物浓度下会产生抑制动力学，但测定的表观Km为2.22 mM。根据金属需求确定了最佳反应条件。酶活性绝对依赖于Triton X-100（0.5%），并受到阳离子和阴离子去污剂的抑制。心磷脂特异性磷脂酶D将三酰基溶血心磷脂转化为溶血磷脂酰甘油和磷脂酸。该酶的比活性比报道的源自微生物的其他膜制剂的比活性大约高100倍。
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