1DZV

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant Y113F/Y209F

Summary for 1DZV

• Entry DOI: 10.2210/pdb1dzv/pdb
• Related: 1DZU 1DZW 1DZX 1DZY 1DZZ 1FUA 2FUA 3FUA 4FUA
• Descriptor: L-fuculose phosphate aldolase, SULFATE ION, BETA-MERCAPTOETHANOL, ... (5 entities in total)
• Functional Keywords: lyase (aldehyde), aldolase (class ii), bacterial l-fucose metabolism, cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde, mutant structure
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 24012.92

Authors

Joerger, A.C.,Schulz, G.E. (deposition date: 2000-03-07, release date: 2000-06-02, Last modification date: 2019-09-25)

Primary citation

Joerger, A.C.,Gosse, C.,Fessner, W.-D.,Schulz, G.E.
Catalytic Action of Fuculose 1-Phosphate Aldolase (Class II) as Derived from Structure-Directed Mutagenesis
Biochemistry, 39:6033-, 2000

PubMed Abstract: 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.

PubMed: 10821675
DOI: 10.1021/BI9927686

Experimental method

X-RAY DIFFRACTION (1.86 Å)