May 28, 1976

Enzymatic synthesis of 2-O-alpha-D-mannopyranosyl-methyl-alpha-D-mannopyranoside by a cell-free particulate system of Mycobacterium smegmatis

Biochimica Et Biophysica Acta
J C Schultz, K Takayama

Abstract

A cell-free particulate enzyme preparation of Mycobacterium smegmatis ATCC 607 catalyzed the transfer of labeled mannose from GDP[14C] mannose to methyl-alpha-D-mannopyranoside (an exogenously added acceptor) to form a product that was characterized to be 2-O-alpha-D[14C] mannopyranosyl-methyl-alpha-D-mannopyranoside. This transmannosylase activity was specific for both the sugar nucleotide donor and methyl monosaccharide acceptor. The reaction was stimulated by the addition of various metal ions and had a pH optimum of 6.0. The apparent Km of this transmannosylase reaction for methyl-alpha-D-mannopyranoside was 35 mM. The possible relationship between this "artificial" mannosyl-transfer system and the "natural" system which leads to the formation of the oligomannosides and glycoproteins is discussed.

  • References4
  • Citations1

Citations

Mentioned in this Paper

Glycoproteins
Disaccharides
Mannose
Enzyme agent
Edetic Acid, Sodium Salt
Methylglycosides
oligomannosides
MGAT4C
Mannosyltransferases
polysaccharide-K

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