Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)

As part of our studies to elucidate the mechanisms by which biotrophic plant pathogens obtain and retain carbon from their plant hosts, we have investigated the properties of the mannitol dehydrogenase (E.C. 1.1.1.67) of Cladosporium fulvum (syn. Fulvia fulva). The enzyme has been purified to near-h...

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Main Authors: Noeldner, P., Coleman, M., Faulks, R., Oliver, Richard
Format: Journal Article
Published: 1994
Online Access:http://hdl.handle.net/20.500.11937/23783
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author Noeldner, P.
Coleman, M.
Faulks, R.
Oliver, Richard
author_facet Noeldner, P.
Coleman, M.
Faulks, R.
Oliver, Richard
author_sort Noeldner, P.
building Curtin Institutional Repository
collection Online Access
description As part of our studies to elucidate the mechanisms by which biotrophic plant pathogens obtain and retain carbon from their plant hosts, we have investigated the properties of the mannitol dehydrogenase (E.C. 1.1.1.67) of Cladosporium fulvum (syn. Fulvia fulva). The enzyme has been purified to near-homogeneity and has a subunit mol. wt of 29 kDa and is probably tetrameric. The Michaelis-Menten constants for mannitol and fructose are high and the equilibrium constant lies towards mannitol accumulation. A β-fructosidase (invertase) activity was detected and found to be largely wall-bound. The properties of these enzymes are consistent with a role in the hydrolysis of photosynthetically produced sucrose and the accumulation of mannitol as a storage compound during fungal growth in the plant.
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spelling curtin-20.500.11937-237832017-09-13T15:58:09Z Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva) Noeldner, P. Coleman, M. Faulks, R. Oliver, Richard As part of our studies to elucidate the mechanisms by which biotrophic plant pathogens obtain and retain carbon from their plant hosts, we have investigated the properties of the mannitol dehydrogenase (E.C. 1.1.1.67) of Cladosporium fulvum (syn. Fulvia fulva). The enzyme has been purified to near-homogeneity and has a subunit mol. wt of 29 kDa and is probably tetrameric. The Michaelis-Menten constants for mannitol and fructose are high and the equilibrium constant lies towards mannitol accumulation. A β-fructosidase (invertase) activity was detected and found to be largely wall-bound. The properties of these enzymes are consistent with a role in the hydrolysis of photosynthetically produced sucrose and the accumulation of mannitol as a storage compound during fungal growth in the plant. 1994 Journal Article http://hdl.handle.net/20.500.11937/23783 10.1016/S0885-5765(05)80059-1 restricted
spellingShingle Noeldner, P.
Coleman, M.
Faulks, R.
Oliver, Richard
Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title_full Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title_fullStr Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title_full_unstemmed Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title_short Purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen Cladosporium fulvum (syn. Fulvia fulva)
title_sort purification and characterization of mannitol dehydrogenase from the fungal tomato pathogen cladosporium fulvum (syn. fulvia fulva)
url http://hdl.handle.net/20.500.11937/23783