Chemical and functional properties of mutastein, an inhibitor of insoluble glucan synthesis by Streptococcus sobrinus.
Mutastein, a potent inhibitor of insoluble glucan synthesis by Streptococcus sobrinus, is a protein with a molecular weight of approximately 2 x 10(6). Amino acid and ELISA analyses suggested that mutastein is a mixture of heterogenous polymers of alpha-casein contained in the culture medium of the producing strain, Aspergillus terreus M3328. Mutastein strongly inhibited the primer-dependent insoluble glucan synthase of S. sobrinus B13. The primer-independent soluble glucan synthase was not affected by mutastein while primer-dependent soluble glucan synthase was slightly activated.
Hayashida
O
O
Department of Applied Biological Science, Faculty of Agriculture, Tokyo Noko University, Japan.
Hasumi
K
K
Endo
A
A
D000596:Amino Acids / Q000032:analysis; D004789:Enzyme Activation; D004797:Enzyme-Linked Immunosorbent Assay; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D005936:Glucans / Q000096:biosynthesis*; D005964:Glucosyltransferases / Q000378:metabolism; D016986:Streptococcus sobrinus / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism
D000596:Amino Acids; D005656:Fungal Proteins; D005936:Glucans; C036864:Mutastein protein, Aspergillus terreus M3328; D005964:Glucosyltransferases; C040232:glucan synthase