Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Galactonate dehydratase"'
Akademický článek
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Publikováno v:
FEMS Microbiology Letters. 367
The haloarchaeon Haloferax volcanii was found to grow on D-galactose as carbon and energy source. Here we report a comprehensive analysis of D-galactose catabolism in H. volcanii. Genome analyses indicated a cluster of genes encoding putative enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19b4ef51ebaa7518ff1cde8607a6b521
https://doi.org/10.1093/femsle/fnaa029
https://doi.org/10.1093/femsle/fnaa029
Akademický článek
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Publikováno v:
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
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 par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e2eaf2860e2a9c42fabd43364f0557e
https://cris.vtt.fi/en/publications/3f98a32e-959f-400b-b9d7-f716ec7e7015
https://cris.vtt.fi/en/publications/3f98a32e-959f-400b-b9d7-f716ec7e7015
Publikováno v:
FEBS Letters. 576:133-136
An investigation has been carried out into gluconate dehydratase from the hyperthermophilic Archaeon Sulfolobus solfataricus. The enzyme has been purified from cell extracts of the organism and found to be responsible for both gluconate and galactona
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a115fe9c0ed4a447a5150dac60d37b6f
https://doi.org/10.1016/j.febslet.2004.08.074
https://doi.org/10.1016/j.febslet.2004.08.074
Autor:
Ali M. Elshafei, Osama M. Abdel-Fatah
Publikováno v:
Enzyme and Microbial Technology. 13:930-934
The abilities of six species of fungi to utilize and degrade d -galactose a the sole carbon source were compared. A nonphosphorolytic pathway for d -galactonate catabolism was found to be operative by a cell-free extract of d -galactonate-grown mycel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f492048c334e53e35f5dae043a2c30dc
https://doi.org/10.1016/0141-0229(91)90111-m
https://doi.org/10.1016/0141-0229(91)90111-m
Publikováno v:
Valkonen, M, Penttilä, M & Benčina, M 2014, ' Intracellular pH responses in the industrially important fungus Trichoderma reesei ', Fungal Genetics and Biology, vol. 70, pp. 86-93 . https://doi.org/10.1016/j.fgb.2014.07.004
Preserving an optimal intracellular pH is critical for cell fitness and productivity. The pH homeostasis of the industrially important filamentous fungus Trichoderma reesei (Hypocrea jecorina) is largely unexplored. We analyzed the impact of growth c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3c61e451db6f1ae79a1b882454e10cb
https://pubmed.ncbi.nlm.nih.gov/25046860
https://pubmed.ncbi.nlm.nih.gov/25046860
Autor:
Ali M. Elshafei, Osama M. Abdel-Fatah
Publikováno v:
Enzyme and Microbial Technology. 29:76-83
Aspergillus niger could utilize D-galactose as sole source of carbon. Cell-free extracts of D-galactose-grown mycelia were able to catalyze the oxidation of D-galactose to D-galactonic acid-gamma-lactone (GalA-gamma-lact) in the presence of NAD, foll
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1aec1d1198685418768cf7912047c98e
https://doi.org/10.1016/s0141-0229(01)00346-5
https://doi.org/10.1016/s0141-0229(01)00346-5
Autor:
Suwen Zhao, Chakrapani Kalyanaraman, Boxue Tian, Matthew P. Jacobson, Leif A. Eriksson, Frank H. Wallrapp
Publikováno v:
Biochemistry, vol 52, iss 33
The stereo-specificity of D-glucarate dehydratase (GlucD) is explored by QM/MM calculations. Both the substrate binding and the chemical steps of GlucD contribute to substrate specificity. Although the identification of transition states remains comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2282303531afb2dfc6bfbf505c9d9f
https://pubmed.ncbi.nlm.nih.gov/23901785
https://pubmed.ncbi.nlm.nih.gov/23901785
Publikováno v:
Antonie van Leeuwenhoek. 67:211-216
Two enzymes catalyze the two step reactions in the D-galactonate nonphosphorolytic catabolic pathway of Aspergillus terreus, namely D-galactonate dehydratase and 2-keto-3-deoxy-D-galactonate (KDGal) aldolase. Maximum enzyme activities were obtained a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20d30b82f05f66befe1223adcbd2642a
https://doi.org/10.1007/bf00871215
https://doi.org/10.1007/bf00871215