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Crucial role of Pro 257 in the thermostability of Bacillus phytases: biochemical and structural investigation
Farhat-Khemakhem A, et al. Int J Biol Macromol 2013. Among authors: Khemakhem B. PMID 23178368
It differs with PhyC from B. subtilis VTTE-68013 by the R257P substitution. PHY US417 was shown to be more thermostable than PhyC. ...
It differs with PhyC from B. subtilis VTTE-68013 by the R257P substitution. PHY US417 was shown to be more thermostable than PhyC. .. …
Toward the smallest active subdomain of a TIM-barrel fold: insights from a truncated α-amylase
Ben Ali M, et al. Biochem Biophys Res Commun 2011. Among authors: Khemakhem B. PMID 21741359
The enzymatic activity can, until now, be attributed to the presence of the whole domain B, in the structure of AmyTM. This mutant revealed, for the first time, the regeneration of a catalytic site after its abolition. ...
The enzymatic activity can, until now, be attributed to the presence of the whole domain B, in the structure of AmyTM. This mutant re …
The importance of an extra loop in the B-domain of an alpha-amylase from B. stearothermophilus US100.
Khemakhem B, et al. Biochem Biophys Res Commun 2009. PMID 19422796
To provide insight into the potential role of a loop in domain B of several bacterial alpha-amylases, molecular and structural investigation of Bacillus stearothermophilus alpha-amylase (Amy US100) was used as a model. ...The structural investigation showed that stabilizing deletions contribute to reinforce the architecture of domain B and the active site conformation. ...
To provide insight into the potential role of a loop in domain B of several bacterial alpha-amylases, molecular and structural invest …
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