Premium
METABOLISM OF MANNITOL IN MYCORRHIZAL AND NON‐MYCORRHIZAL FUNGI
Author(s) -
RAMSTEDT MAURITZ,
JIRJIS RAIDA,
SÖDERHÄLL KENNETH
Publication year - 1987
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1987.tb00865.x
Subject(s) - mannitol , dehydrogenase , biochemistry , ectomycorrhiza , phosphate , mycorrhiza , phosphatase , biology , chemistry , enzyme , bacteria , symbiosis , genetics
S ummary The activity of mannitol dehydrogenase, mannitol 1‐phosphatase and mannitol 1‐phosphate dehydrogenase in five mycorrhizal basidiomycetes, one mycorrhizal ascomycete and five non‐mycorrhizal basidiomycetes was investigated. No mannitol 1‐phosphate dehydrogenase could be detected in any of the basidiomycetes. Mannitol dehydrogenase, present in all the tested fungi except Armillariella mellea , was strictly NAD‐dependent for the non‐mycorrhizal basidiomycetes, whereas in the mycorrhizal species it was mainly NADP‐dependent. The mannitol 1‐phosphatase of the mycorrhizal basidiomycetes was specific towards mannitol 1‐phosphate in contrast to that of the non‐mycorrhizal species, which was a non‐specific phosphatase. In the ascomycete Sphaerosporella brunnea all the mannitol metabolizing enzymes were found, including mannitol 1‐phosphate dehydrogenase. Growth of S. brunnea on mannitol slightly decreased the activity of the mannitol dehydrogenase (NADP) and mannitol 1‐phosphate dehydrogenase, but there was a slight increase in activity of glucose 6‐phosphate dehydrogenase.