NDLI: Ammonia assimilation in Corynebacterium glutamicum and a glutamate dehydrogenase-deficient mutant

Content Provider	Springer Nature Link
Author	Tesch, Martin Eikmanns, Bernhard J. de Graaf, Albert A. Sahm, Hermann
Copyright Year	1998
Abstract	In the wild-type of Corynebacterium glutamicum, the specific activity of glutamate dehydrogenase (GDH) remained constant at 1.3 U (mg protein)−1 when raising the ammonia (NH4) concentration in the growth medium from 1 to 90 mM. In contrast, the glutamine synthetase (GS) and glutamate synthase (GOGAT) activities decreased from 1.1 U (mg protein)−1 and 42 mU (mg protein)−1, respectively, to less than 10 % of these values at NH4 concentrations > 10 mM suggesting that under these conditions the GDH reaction is the primary NH4 assimilation pathway. Consistent with this suggestion, a GDH-deficient C. glutamicum mutant showed slower growth at NH4 concentrations ≥ 10 mM and, in contrast to the wild-type, did not grow in the presence of the GS inhibitor methionine sulfoximine. © Rapid Science Ltd. 1998
Starting Page	953
Ending Page	957
Page Count	5
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	20
Issue Number	10
e-ISSN	15736776
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Organic Chemistry Biochemistry Microbiology Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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Ammonia assimilation in Corynebacterium glutamicum and a glutamate dehydrogenase-deficient mutant