期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 74, 期 1-2, 页码 97-102出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2011.09.004
关键词
1,3-beta-Galactosyl-N-acetylhexosamine phosphorylase; Glycoside hydrolase family 112; Galacto-N-biose; Lacto-N-biose I; Determinant residue of substrate preference
资金
- Program for Promotion of Basic Research Activities for Innovative biosciences (PROBRAIN)
Three amino acid residues of 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (GalHexNAcP) were assigned as the determinants of substrate preference for galacto-N-biose (GNB) and lacto-N-biose I (LNB) based on the three-dimensional structure of the protein. Mutants of GalHexNAcP from Bifidobacterium longum, which acts similarly on both GNB and LNB, were constructed and characterized. V162T mutation led to an increase in the selectivity on GNB. P161S and S336A mutations independently enhanced the selectivity on LNB. The alignment of amino acid sequences suggests that the activities of most homologous sequences are predictable by comparing the corresponding three residues. (C) 2011 Elsevier B.V. All rights reserved.
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