Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate

Proteins. 2007 Nov 1;69(2):433-9. doi: 10.1002/prot.21602.
No abstract available

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Validation Study

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / enzymology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology
  • Crystallography, X-Ray
  • Hydrolysis
  • Molecular Sequence Data
  • Organophosphates / chemistry
  • Organophosphates / metabolism*
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / physiology*
  • Thioglycosides / chemistry
  • Thioglycosides / metabolism*

Substances

  • 5-methylthiopentose
  • Bacterial Proteins
  • Organophosphates
  • Thioglycosides
  • Phosphoric Monoester Hydrolases