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Prediction of structure and functional residues for O ‐GlcNAcase, a divergent homologue of acetyltransferases
Author(s) -
Schultz Jörg,
Pils Birgit
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03322-7
Subject(s) - acetyltransferases , protein superfamily , biochemistry , protein family , histone acetyltransferases , posttranslational modification , biology , archaea , enzyme , protein structure , chemistry , computational biology , acetylation , gene
N ‐Acetyl‐β‐ D ‐glucosaminidase ( O ‐GlcNAcase) is a key enzyme in the posttranslational modification of intracellular proteins by O ‐linked N ‐acetylglucosamine ( O ‐GlcNAc). Here, we show that this protein contains two catalytic domains, one homologous to bacterial hyaluronidases and one belonging to the GCN5‐related family of acetyltransferases (GNATs). Using sequence and structural information, we predict that the GNAT homologous region contains the O ‐GlcNAcase activity. Thus, O ‐GlcNAcase is the first member of the GNAT family not involved in transfer of acetyl groups, adding a new mode of evolution to this large protein family. Comparison with solved structures of different GNATs led to a reliable structure prediction and mapping of residues involved in binding of the GlcNAc‐modified proteins and catalysis.