1DZY

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant E214A

1DZY の概要

• エントリーDOI: 10.2210/pdb1dzy/pdb
• 関連するPDBエントリー: 1DZU 1DZV 1DZW 1DZX 1DZZ 1FUA 2FUA 3FUA 4FUA
• 分子名称: L-FUCULOSE-1-PHOSPHATE ALDOLASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (5 entities in total)
• 機能のキーワード: lyase (aldehyde), aldolase (class ii), bacterial l-fucose metabolism, cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde, mutant structure
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24082.95

構造登録者

Joerger, A.C.,Schulz, G.E. (登録日: 2000-03-07, 公開日: 2000-06-02, 最終更新日: 2025-04-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.44 Å)