Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties
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چکیده
منابع مشابه
Sequence heterogeneity between the two genes encoding 16S rRNA from the halophilic archaebacterium Haloarcula marismortui.
The halophilic archaebacterium, Haloarcula marismortui, contains two nonadjacent ribosomal RNA operons, designated rrnA and rrnB, in its genome. The 16S rRNA genes within these operons are 1472 nucleotides in length and differ by nucleotide substitutions at 74 positions. The substitutions are not uniformly distributed but rather are localized within three domains of 16S rRNA; more than two-thir...
متن کاملCrystal Structure of Cruxrhodopsin-3 from Haloarcula vallismortis
Cruxrhodopsin-3 (cR3), a retinylidene protein found in the claret membrane of Haloarcula vallismortis, functions as a light-driven proton pump. In this study, the membrane fusion method was applied to crystallize cR3 into a crystal belonging to space group P321. Diffraction data at 2.1 Å resolution show that cR3 forms a trimeric assembly with bacterioruberin bound to the crevice between neighbo...
متن کاملThe purification and properties of human liver ketohexokinase. A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol.
Ketohexokinase (EC 2.7.1.3) was purified to homogeneity from human liver, and fructose-bisphosphate aldolase (EC 4.1.2.13) was partially purified from the same source. Ketohexokinase was shown, by column chromatography and polyacrylamide-gel electrophoresis, to be a dimer of Mr 75000. Inhibition studies with p-chloromercuribenzoate and N-ethylmaleimide indicate that ketohexokinase contains thio...
متن کاملPurification and properties of a nucleoside phosphotransferase from carrot.
A simple procedure affording a 940-fold purification of the nucleoside phosphotransferase from carrot is described. Preliminary evidence indicates that, by an additional fractionation through a Sephadex column, a further 5to 6-fold increase in activity can be effected. The particle weight of the enzyme varies with pH. At the pH optimum of 5.0 one species of particle weight 45,000, at pH 9.5 two...
متن کاملStructural features that stabilize halophilic malate dehydrogenase from an archaebacterium.
The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1994
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.176.17.5505-5512.1994