Abstract：
:Dihydroxyacetone (DHA) kinase from Citrobacter freundii provides an easy entry for the preparation of DHA phosphate; a very important C3 building block in nature. To modify the phosphoryl donor specificity of this enzyme from ATP to inorganic polyphosphate (poly-P); a directed evolution program has been initiated. In the first cycle of evolution, the native enzyme was subjected to one round of error-prone PCR (EP-PCR) followed directly (without selection) by a round of DNA shuffling. Although the wild-type DHAK did not show activity with poly-P, after screening, sixteen mutant clones showed an activity with poly-phosphate as phosphoryl donor statistically significant. The most active mutant presented a single mutation (Glu526Lys) located in a flexible loop near of the active center. Interestingly, our theoretical studies, based on molecular dynamics simulations and hybrid Quantum Mechanics/Molecular Mechanics (QM/MM) optimizations, suggest that this mutation has an effect on the binding of the poly-P favoring a more adequate position in the active center for the reaction to take place.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Sánchez-Moreno I,Bordes I,Castillo R,Ruiz-Pernía JJ,Moliner V,García-Junceda Edoi
10.3390/ijms161126073subject
Has Abstractpub_date
2015-11-24 00:00:00pages
27835-49issue
11issn
1422-0067pii
ijms161126073journal_volume
16pub_type
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