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- W2052835643 abstract "The three-dimensional structure of L-fuculose-1-phosphate aldolase (FucA) from Escherichia coli was determined by X-ray crystallography at a resolution of 2.13 A. The enzyme is a homotetramer with an M(r) of 23,775 per subunit. Since its activity depends on the presence of metal ions (Zn2+) the enzyme belongs to the class II aldolases. As expected from amino acid sequence comparisons, this first structure of a class II aldolase shows no similarity to the known structures of class I aldolases. It has some unusual features concerning the overall chain fold, the quaternary structure, and the co-ordination of the catalytically active zinc ion. A sequence comparison with the data bank indicated that the middle domain of the enzyme L-ribulose-5-phosphate-4-epimerase is homologous to FucA and may contain an active-center metal ion." @default.
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- W2052835643 date "1993-06-01" @default.
- W2052835643 modified "2023-10-13" @default.
- W2052835643 title "The Spatial Structure of the Class II l-Fuculose-1-phosphate Aldolase from Escherichia coli" @default.
- W2052835643 doi "https://doi.org/10.1006/jmbi.1993.1307" @default.
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