纯化和表征phosphomannomutase / phosphoglucomutase从铜绿假单胞菌海藻酸和脂多糖的生物合成。
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你们RW, Zielinski NA, Chakrabarty有空
纯化和表征phosphomannomutase / phosphoglucomutase从铜绿假单胞菌海藻酸和脂多糖的生物合成。
J Bacteriol。1994年8月,176 (16):4851 - 7。
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8050998 (在PubMed]
- 文摘
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algC基因从铜绿假单胞菌已被证明编码phosphomannomutase (PMM),海藻酸生物合成的关键酶和脂多糖(LPS)。这个基因过表达tac启动子的控制下,酶的纯化及其底物特异性和金属离子的影响特征。酶被确定为单体的分子质量50 kDa。甘露糖的酶催化互变现象1-phosphate (M1P)和甘露糖6-phosphate,以及葡萄糖1-phosphate (G1P)和葡萄糖6-phosphate。明显的Km值M1P和G1P microM 17日和22日,分别。Kcat /公里比的基础上,催化效率高于M1P G1P是双重的。PMM也催化转换核糖1-phosphate和2-deoxyglucose 6-phosphate相应的同分异构体,虽然活动是低得多。纯化PMM / phosphoglucomutase (PGM)要求Mg2 +最大活动;Mn2 +是唯一的其他二价金属显示一些激活。其他二价金属的存在除了Mg2 +反应抑制酶活性。 PMM and PGM activities could not be detected in nonmucoid algC mutant strain 8858 and in LPS-rough algC mutant strain AK1012, while they were present in the wild-type strains as well as in algC-complemented mutant strains. This evidence suggests that AlgC functions as PMM and PGM in vivo, converting phosphomannose and phosphoglucose in the biosynthesis of both alginate and LPS.