Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD(+)/Mn2+-dependent phospho-alpha-glucosidase from Bacillus subtilis

S S Rajan, X J Yang, F Collart, V L Y Yip, S G Withers, A Varrot, J Thompson, G J Davies, W F Anderson

Research output: Contribution to journalArticlepeer-review

Abstract

GlvA, a 6-phospho-alpha-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6'-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 Angstrom resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

Original languageEnglish
Pages (from-to)1619-1629
Number of pages11
JournalStructure
Volume12
Issue number9
DOIs
Publication statusPublished - Sept 2004

Keywords

  • GLUCOSYL-D-FRUCTOSES
  • CRYSTAL-STRUCTURE
  • THERMOTOGA-MARITIMA
  • ESCHERICHIA-COLI
  • FAMILY 4
  • KLEBSIELLA-PNEUMONIAE
  • HIGH-THROUGHPUT
  • DEHYDROGENASE
  • REFINEMENT
  • ASSIGNMENT

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