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

Shyamala S. Rajan, Xiaojing Yang, Frank Collart, Vivian L.Y. Yip, Stephen G. Withers, Annabelle Varrot, John Thompson, Gideon J. Davies, Wayne F. Anderson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

GlvA, a 6-phospho-α-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 Å 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 (US)
Pages (from-to)1619-1629
Number of pages11
JournalStructure
Volume12
Issue number9
DOIs
StatePublished - Sep 2004

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD<sup>+</sup>/Mn<sup>2+</sup>-dependent phospho-α-glucosidase from Bacillus subtilis'. Together they form a unique fingerprint.

Cite this