Inorganic pyrophosphatase activity in cell-free extracts of Ureaplasma urealyticum.
Inorganic pyrophosphatase activity in cell-free extracts of Ureaplasma urealyticum.
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解脲脲原体无细胞提取物中的无机焦磷酸酶活性。
DOI：
10.1099/00221287-133-6-1453
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Ortiz,R
中科院分区：
文献类型：
--
作者：
DavisJr,JW;Moses,IS;Ndubuka,C;Ortiz,R
解脲脲原体菌株Pi和T960（CX 8）（分别为血清型6和8）的无细胞提取物代谢无机焦磷酸盐（PPi）。无机焦磷酸酶（PPase）活性最高，Mg ~（2+）为辅因子，Mn ~（2+）为弱替代物。两种血清型的PP酶在遗传学上不同。尽管使用PPias底物获得最高的PPase活性，但该酶也可以在较小程度上利用三聚磷酸盐和三偏磷酸盐。未观察到对β-甘油磷酸、萘基磷酸、葡萄糖6-磷酸、果糖6-磷酸、果糖1，6-二磷酸、硫胺素焦磷酸、磷酸核糖基焦磷酸、ADP或ATP的活性。以磷酸萘酯为底物，观察到酸性和碱性磷酸酶活性，但它们在凝胶上的电泳迁移率与PPase活性不同。氧化型谷胱甘肽、1-乙基-3-（3-二甲氨基丙基）碳二亚胺、苯基乙二醛、对氯汞苯甲酸、Mn ~（2+）、Zn ~（2+）和Ca ~（2+）对尿素解磷酶有抑制作用。无论是还原型谷胱甘肽，L-半胱氨酸，也没有Co2+增强活性。PPican作为某些代谢反应的底物或调节剂，PPi代谢可以在细菌生物能量学中发挥作用;其在脲原体中的作用目前尚不清楚。
Cell-free extracts ofUreaplasma urealyticumstrains Pi and T960 (CX8) (serovars 6 and 8, respectively) metabolized inorganic pyrophosphate (PPi). The inorganic pyrophosphatase (PPase) activity was greatest with Mg2+as cofactor, but Mn2+acted as a poor substitute. The PPases of the two serovars differed electrophoretically. Although the highest PPase activity was obtained using PPias substrate, the enzyme could also utilize to a lesser degree both tripolyphosphate and trimetaphosphate. No activity was observed against β-glycerophosphate, naphthyl phosphates, glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, thiamin pyrophosphate, phosphoribosylpyrophosphate, ADP or ATP. Acid- and alkaline-phosphatase activities were observed with naphthyl phosphates as substrates, but they did not have the same electrophoretic mobility on gels as the PPase activity.U. urealyticumPPase was inhibited by oxidized glutathione, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, phenyl-glyoxal,p-chloromercuribenzoic acid, Mn2+, Zn2+and Ca2+. Neither reduced glutathione,l-cysteine nor Co2+enhanced activity. PPican act as a substrate or regulator of certain metabolic reactions, and PPimetabolism can function in bacterial bioenergetics; its role in ureaplasmas is presently unclear.