1dzy: Difference between revisions

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[[Image:1dzy.jpg|left|200px]]
{{Seed}}
[[Image:1dzy.png|left|200px]]


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{{STRUCTURE_1dzy|  PDB=1dzy  |  SCENE=  }}  
{{STRUCTURE_1dzy|  PDB=1dzy  |  SCENE=  }}  


'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E214A'''
===L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E214A===




==Overview==
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Previous analyses established the structures of unligated L-fuculose 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking the substrate dihydroxyacetone phosphate. These data allowed us to suggest a catalytic mechanism. On the basis of this proposal, numerous mutations were now introduced at the active center and tested with respect to their catalytic rates and their product distributions. For several mutants, the structures were determined. The results demonstrate the catalytic importance of some particular residues in defined conformations and in the mobile C-terminal chain end. Moreover, they led to a modification of the proposed mechanism. The effect of some mutations on enantioselectivity and on the ratio of diastereomer formation indicates clearly the binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
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{{ABSTRACT_PUBMED_10821675}}


==About this Structure==
==About this Structure==
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[[Category: Cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
[[Category: Cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
[[Category: Mutant structure]]
[[Category: Mutant structure]]
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