Publications by authors named "A B Teplitsky"

Background: Several studies have shown that delay in neurosurgical intervention worsens the neurologic outcome. However, rapid evacuation of wounded sustaining intracranial injury (ICI) to the nearest hospital may have some advantages, as the nearest hospital ER may be a better environment to prevent a secondary brain injury than the ambulance. Also, evacuation to a referral centre of all the wounded suspected in the field to have ICI will result in high rates of over triage.

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Geobacillus stearothermophilus T-6 is a thermophilic Gram-positive bacterium that produces two selective family 10 xylanases which both take part in the complete degradation and utilization of the xylan polymer. The two xylanases exhibit significantly different substrate specificities. While the extracellular xylanase (XT6; MW 43.

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The extracellular thermostable xylanase (XT-6) produced by the thermophilic bacterium Bacillus stearothermophilus T-6 was shown to bleach pulp optimally at pH 9 and 338 K, and was successfully used in a large-scale biobleaching mill trial. The xylanase gene was cloned and sequenced. The mature enzyme consists of 379 amino acids with a calculated molecular weight of 43,808 and pI of 9.

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Xylanases are hemicellulases that hydrolyze the internal beta-1,4-glycoside bonds of xylan. The extracellular thermostable endo-1,4-beta-xylanase (EC 3.2.

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Article Synopsis
  • Alpha-glucuronidases break down hemicellulose by cleaving specific bonds in xylooligomers, and are classified under family 67 glycosidases that operate through a unique hydrolysis mechanism.
  • The study presents detailed crystal structures of the alpha-glucuronidase (AguA) from Geobacillus stearothermophilus, revealing how the enzyme interacts with its substrate and products at a molecular level.
  • Key structural features include a distorted sugar ring that facilitates a transition state for the reaction, and the activation of a nucleophilic water molecule by two carboxylic acids, indicating a novel substrate-assisted catalytic mechanism involving the general acid Gl
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