Identification of Asp197 as the catalytic nucleophile in the family 38 alpha-mannosidase from bovine kidney lysosomes

FEBS Lett. 2000 Nov 10;484(3):175-8. doi: 10.1016/s0014-5793(00)02148-7.

Abstract

Bovine kidney lysosomal alpha-mannosidase is a family 38 alpha-mannosidase involved in the degradation of glycoproteins. The mechanism-based reagent, 5-fluoro-beta-L-gulosyl fluoride, was used to trap a glycosyl-enzyme intermediate, thereby labelling the catalytic nucleophile of this enzyme. After proteolytic digestion and high performance liquid chromatography/tandem mass spectrometry (MS) analysis, a labelled peptide was localised, and the sequence: HIDPFGHSRE determined by fragmentation tandem MS analysis. Taking into consideration sequence alignments of this region with those of other alpha-mannosidases of the same family, this result strongly suggests that the catalytic nucleophile in this enzyme is Asp197.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartic Acid*
  • Binding Sites
  • Catalytic Domain
  • Cattle
  • Chromatography, High Pressure Liquid
  • Humans
  • Kidney / enzymology*
  • Kinetics
  • Lysosomes / enzymology*
  • Mannosidases / chemistry*
  • Mannosidases / metabolism*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Rats
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Swine
  • alpha-Mannosidase

Substances

  • Aspartic Acid
  • Mannosidases
  • alpha-Mannosidase