Unliganded Acetate Kinase from Thermatoga Maritima
نویسندگان
چکیده
منابع مشابه
Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR.
Molecular dynamics simulations of the temperature-induced unfolding reaction of native dimeric dihydrofolate reductase from the hyperthermophile Thermatoga maritima (TmDHFR) and the experimentally inaccessible TmDHFR monomer were carried out at 400 K, 450 K and 500 K. The results revealed that the unfolding of TmDHFR subunits followed a similar path to that of the monomeric DHFR from the mesoph...
متن کاملPurification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima.
Phosphate acetyltransferase (PTA) and acetate kinase (AK) of the hyperthermophilic eubacterium Thermotoga maritima have been purified 1,500- and 250-fold, respectively, to apparent homogeneity. PTA had an apparent molecular mass of 170 kDa and was composed of one subunit with a molecular mass of 34 kDa, suggesting a homotetramer (alpha4) structure. The N-terminal amino acid sequence showed sign...
متن کاملPhosphorylated Acetate Kinase
Acetate kinase (ATP: acetate phosphotransferase, EC 2.7.2.1) can be phosphorylated with ATP or with acetyl phosphate. The degree of phosphorylation increases with the relative concentration of phosphorylating agent. The isolated phosphoenzyme reacts quantitatively with ADP to form ATP, and with acetate to form acetyl phosphate in 70 to 80 % yield. The pH stability profile of the phosphoenzyme a...
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From the chloroform extract of the fresh fruits of Diospyros maritima BLUME (Ebenaceae), five new naphthoquinone derivatives, 2,7'-dimethyl-2',3-bijuglone (27), 2,7'-dimethyl-3,3'-bijuglone (28), 2,7'-dimethyl-6,8'-bijuglone (29), 7,7'-dimethyl-3,3'-ethylidenebijuglone (30), and 2',7-dimethyl-3,6'-ethylidenebijuglone (31), were isolated, in addition to twenty-one known naphthoquinone derivative...
متن کاملNovel pyrophosphate-forming acetate kinase from the protist Entamoeba histolytica.
Acetate kinase (ACK) catalyzes the reversible synthesis of acetyl phosphate by transfer of the γ-phosphate of ATP to acetate. Here we report the first biochemical and kinetic characterization of a eukaryotic ACK, that from the protist Entamoeba histolytica. Our characterization revealed that this protist ACK is the only known member of the ASKHA structural superfamily, which includes acetate ki...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2006
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.20.5.lb59-a