L-galactonate dehydratase is part of the fungal path for D-galacturonic acid catabolism

Autor: Merja Penttilä, Paula Jouhten, Peter Richard, Satu Kuorelahti, Hannu Maaheimo
Jazyk: angličtina
Rok vydání: 2006
Předmět:
Zdroj: Kuorelahti, S, Jouhten, P, Maaheimo, H, Penttilä, M & Richard, P 2006, ' L-galactonate dehydratase is part of the fungal path for D-galacturonic acid catabolism ', Molecular Microbiology, vol. 61, no. 4, pp. 1060-1068 . https://doi.org/10.1111/j.1365-2958.2006.05294.x
ISSN: 1365-2958
0950-382X
DOI: 10.1111/j.1365-2958.2006.05294.x
Popis: An L-galactonate dehydratase and the corresponding gene were identified from the mould Hypocrea jecorina (Trichoderma reesei). This novel enzyme converts L-galactonate to L-threo-3-deoxy-hexulosonate (2-keto-3-deoxy-L- galactonate). The enzyme is part of the fungal pathway for D-galacturonic acid catabolism, a pathway which is only partly known. It is the second enzyme of this pathway after the D-galacturonic acid reductase. L-galactonate dehydratase activity is present in H. jecorina cells grown on D-galacturonic acid but absent when other carbon sources are used for growth. A deletion of the L-galactonate dehydratase gene in H. jecorina results in a strain with no growth on D-galacturonic acid. The active enzyme was produced in the heterologous host Saccharomyces cerevisiae and characterized. It exhibited activity with L-galactonate and D-arabonate where the hydroxyl group of the C2 is in L- and the hydroxyl group of the C3 is in D-configuration in the Fischer projection. However, it did not exhibit activity with D-galactonate, D-gluconate, L-gulonate or D-xylonate where the hydroxyl groups of the C2 and C3 are in different configuration.
Databáze: OpenAIRE