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- W2090130229 abstract "Comparison of the recently determined crystal structures Pseudomonas fluorescens subsp. cellulosa family F xylanase, (1–3)-β-glucanase and (1–3,1–4)-β-glucanase and the catalytic domain of E. coli β-galactosidase reveals that they belong to a superfamily of 8-fold β/α-barrels with similar amino acid residues at their active sites. In the three families that these enzymes represent, the nucleophile is a glutamate, which is located close to the carboxy-terminus of β-strand seven. In addition all three enzymes have the sequence asparagine-glutamate close to the carboxy-terminus of β-strand four. This glutamate has been identified as the acid/base in the family F xylanases and is essential for catalysis in β-galactosidase. We suggest that the equivalent residue in the barley glucanases is the acid/base. Analysis of the sequences of family 1 β-glucosidases and family 5 cellulases shows that these enzymes also belong to this superfamily which we call the 47 superfamily." @default.
- W2090130229 created "2016-06-24" @default.
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- W2090130229 date "1983-11-01" @default.
- W2090130229 modified "2023-09-26" @default.
- W2090130229 title "Molecular structure and biological activity" @default.
- W2090130229 doi "https://doi.org/10.1016/0968-0004(83)90315-8" @default.
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