Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus

The glutamate dehydrogenase gene of Escherichia coli has been cloned into broad host-range plasmids and can complement glutamate synthase mutants of Methylophilus methylotrophus. Assimilation of ammonia via glutamate dehydrogenase is more energy-efficient than via glutamate synthase, thus the recomb...

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Bibliographic Details
Published inNature (London) Vol. 287; no. 5781; p. 396
Main Authors Windass, J D, Worsey, M J, Pioli, E M, Pioli, D, Barth, P T, Atherton, K T, Dart, E C, Byrom, D, Powell, K, Senior, P J
Format Journal Article
LanguageEnglish
Published England 02.10.1980
Subjects
Adenosine Triphosphate - metabolism
Ammonia - metabolism
Bacterial Proteins - biosynthesis
DNA, Recombinant
Escherichia coli - enzymology
Genetic Engineering - methods
Glutamate Dehydrogenase - genetics
Glutamate Synthase - metabolism
Methanol - metabolism
Methylococcaceae - enzymology
Methylococcaceae - metabolism
Plasmids
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Summary:The glutamate dehydrogenase gene of Escherichia coli has been cloned into broad host-range plasmids and can complement glutamate synthase mutants of Methylophilus methylotrophus. Assimilation of ammonia via glutamate dehydrogenase is more energy-efficient than via glutamate synthase, thus the recombinant organism converts more growth substrate, methanol, into cellular carbon.
ISSN:0028-0836
1476-4687
DOI:10.1038/287396a0