1dzz: Difference between revisions

Revision as of 23:54, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dzz.png

Template:STRUCTURE 1dzz

L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113FL-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F

Template:ABSTRACT PUBMED 10821675

About this StructureAbout this Structure

1DZZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis., Joerger AC, Gosse C, Fessner WD, Schulz GE, Biochemistry. 2000 May 23;39(20):6033-41. PMID:10821675

Page seeded by OCA on Mon Jun 30 23:54:41 2008

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OCA

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-'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F'''
+===L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10821675}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10821675 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10821675}}
 ==About this Structure==
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 [[Category: Cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
 [[Category: Mutant structure]]
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