Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

Mamoru Nishimoto, Masafumi Hidaka, Masahiro Nakajima, Shinya Fushinobu, Motomitsu Kitaoka

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Three amino acid residues of 1,3-β-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. .

Original languageEnglish
Pages (from-to)97-102
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume74
Issue number1-2
DOIs
Publication statusPublished - 2012 Jan 1

Keywords

  • 1,3-β-Galactosyl-N-acetylhexosamine phosphorylase
  • Determinant residue of substrate preference
  • Galacto-N-biose
  • Glycoside hydrolase family 112
  • Lacto-N-biose I

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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