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首页> 外文期刊>Journal of bacteriology >Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties.
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Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties.

机译：来自嗜盐古细菌Haloarcula vallismortis的酮己糖激酶（ATP：D-果糖1-磷酸转移酶）：纯化和性质。

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摘要

Ketohexokinase (ATP:D-fructose 1-phosphotransferase [EC 2.7.1.3]), detected for the first time in a prokaryote, i.e., the extreme halophile Haloarcula vallismortis, was isolated and characterized from the same archaebacterium. This enzyme was characterized with respect to its molecular mass, amino acid composition, salt dependency, immunological cross-reactivity, and kinetic properties. Gel filtration and sucrose density gradient centrifugation revealed a native molecular mass of 100 kDa for halobacterial ketohexokinase, which is larger than its mammalian counterpart. The enzyme could be labeled by UV irradiation in the presence of [ gamma-32P]ATP, suggesting the involvement of a phosphoenzyme intermediate. Other catalytic features of the enzyme were similar to those of its mammalian counterparts. No antigenic cross-reactivity could be detected between the H. vallismortis ketohexokinase and the ketohexokinases from different rat tissues.
机译：在原核生物中首次检测到的酮己糖激酶（ATP：D-果糖1-磷酸转移酶[EC 2.7.1.3]）是从同一古细菌中分离并鉴定的。对该酶的分子量，氨基酸组成，盐依赖性，免疫交叉反应性和动力学性质进行了表征。凝胶过滤和蔗糖密度梯度离心显示，盐细菌酮己酮激酶的天然分子量为100 kDa，大于哺乳动物的分子量。可以在[γ-32P] ATP的存在下通过紫外线照射来标记该酶，这表明磷酸酶中间体的参与。该酶的其他催化特性与哺乳动物的相似。在来自不同大鼠组织的戊型肝炎球菌脱氧核糖核酸酶与酮脱氧核糖核酸酶之间未检测到抗原交叉反应。

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