Amylomaltase of Pyrobaculum aerophilum IM2 Produces Thermoreversible Starch Gels
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چکیده
منابع مشابه
Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels.
Amylomaltases are 4-alpha-glucanotransferases (EC 2.4.1.25) of glycoside hydrolase family 77 that transfer alpha-1,4-linked glucans to another acceptor, which can be the 4-OH group of an alpha-1,4-linked glucan or glucose. The amylomaltase-encoding gene (PAE1209) from the hyperthermophilic archaeon Pyrobaculum aerophilum IM2 was cloned and expressed in Escherichia coli, and the gene product (Py...
متن کاملnitrate - reducing hyperthermophilic archaeum . Pyrobaculum aerophilum sp . nov
A novel rod-shaped hyperthermophilic archaeum has been isolated from a boiling marine water hole at Maronti Beach, Ischia, Italy. It grew optimally at 100°C and pH 7.0 by aerobic respiration as well as by dissimilatory nitrate reduction, forming dinitrogen as a final product. Organic and inorganic compounds served as substrates during aerobic and anaerobic respiration. Growth was inhibited by e...
متن کاملPhysicochemical Characterization of a Thermostable Alcohol Dehydrogenase from Pyrobaculum aerophilum
In this work we characterize an alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Pyrobaculum aerophilum (PyAeADHII). We have previously found that PyAeADHII has no activity when standard ADH substrates are used but is active when α-tetralone is used as substrate. Here, to gain insights into enzyme function, we screened several chemical libraries for enzymatic modulators using an ...
متن کاملA thermostable endonuclease III homolog from the archaeon Pyrobaculum aerophilum.
Pyrimidine adducts in cellular DNA arise from modification of the pyrimidine 5,6-double bond by oxidation, reduction or hydration. The biological outcome includes increased mutation rate and potential lethality. A major DNA N:-glycosylase responsible for the excision of modified pyrimidine bases is the base excision repair (BER) glycosylase endonuclease III, for which functional homologs have b...
متن کاملGenome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.
We determined and annotated the complete 2.2-megabase genome sequence of Pyrobaculum aerophilum, a facultatively aerobic nitrate-reducing hyperthermophilic (T(opt) = 100 degrees C) crenarchaeon. Clues were found suggesting explanations of the organism's surprising intolerance to sulfur, which may aid in the development of methods for genetic studies of the organism. Many interesting features wo...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2005
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.71.9.5098-5106.2005