PMID:7729513
| Citation |
Jenkins, J, Lo Leggio, L, Harris, G and Pickersgill, R (1995) Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven. FEBS Lett. 362:281-5 |
|---|---|
| Abstract |
Comparison of the recently determined crystal structures Pseudomonas fluorescens subsp. cellulosa family F xylanase, (1-3)-beta-glucanase and (1-3,1-4)-beta-glucanase and the catalytic domain of E. coli beta-galactosidase reveals that they belong to a superfamily of 8-fold beta/alpha-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 beta-strand seven. In addition all three enzymes have the sequence asparagine-glutamate close to the carboxy-terminus of beta-strand four. This glutamate has been identified as the acid/base in the family F xylanases and is essential for catalysis in beta-galactosidase. We suggest that the equivalent residue in the barley glucanases is the acid/base. Analysis of the sequences of family 1 beta-glucosidases and family 5 cellulases shows that these enzymes also belong to this superfamily which we call the 4/7 superfamily. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Cellulase/chemistry; Endo-1,4-beta Xylanases; Escherichia coli/enzymology; Glucan 1,3-beta-Glucosidase; Glutamates/chemistry; Glycoside Hydrolases/chemistry; Glycoside Hydrolases/genetics; Hordeum/enzymology; Models, Molecular; Molecular Sequence Data; Protein Conformation; Pseudomonas fluorescens/enzymology; Sequence Alignment; Xylosidases/chemistry; Xylosidases/genetics; beta-Galactosidase/chemistry; beta-Glucosidase/chemistry |
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