This title appears in the Scientific Report :
2004
Please use the identifier:
http://dx.doi.org/10.1128/AEM.70.12.7148-7155.2004 in citations.
Please use the identifier: http://hdl.handle.net/2128/2418 in citations.
Co-metabolism of a Non-Growth Substrate: L-Serine Utilization by Corynebacterium glutamicum
Co-metabolism of a Non-Growth Substrate: L-Serine Utilization by Corynebacterium glutamicum
Despite its key position in central metabolism, L-serine does not support the growth of Corynebacterium glutamicum. Nevertheless, during growth on glucose, L-serine is consumed at rates up to 19.4 +/- 4.0 nmol min(-1) (mg [dry weight])(-1), resulting in the complete consumption of 100 mM L-serine in...
Saved in:
Personal Name(s): | Netzer, R. |
---|---|
Peters-Wendisch, P. / Eggeling, L. / Sahm, H. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | Applied and environmental microbiology, 70 (2004) S. 7148 - 7155 |
Imprint: |
Washington, DC [u.a.]
Soc.
2004
|
Physical Description: |
7148 - 7155 |
PubMed ID: |
15574911 |
DOI: |
10.1128/AEM.70.12.7148-7155.2004 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Applied and Environmental Microbiology
70 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/2418 in citations.
Despite its key position in central metabolism, L-serine does not support the growth of Corynebacterium glutamicum. Nevertheless, during growth on glucose, L-serine is consumed at rates up to 19.4 +/- 4.0 nmol min(-1) (mg [dry weight])(-1), resulting in the complete consumption of 100 mM L-serine in the presence of 100 mM glucose and an increased growth yield of about 20%. Use of 13C-labeled L-serine and analysis of cellularly derived metabolites by nuclear magnetic resonance spectroscopy revealed that the carbon skeleton of L-serine is mainly converted to pyruvate-derived metabolites such as L-alanine. The sdaA gene was identified in the genome of C. glutamicum, and overexpression of sdaA resulted in (i) functional L-serine dehydratase (L-SerDH) activity, and therefore conversion of L-serine to pyruvate, and (ii) growth of the recombinant strain on L-serine as the single substrate. In contrast, deletion of sdaA decreased the L-serine cometabolism rate with glucose by 47% but still resulted in degradation of L-serine to pyruvate. Cystathionine beta-lyase was additionally found to convert L-serine to pyruvate, and the respective metC gene was induced 2.4-fold under high internal L-serine concentrations. Upon sdaA overexpression, the growth rate on glucose is reduced 36% from that of the wild type, illustrating that even with glucose as a single substrate, intracellular L-serine conversion to pyruvate might occur, although probably the weak affinity of L-SerDH (apparent Km, 11 mM) prevents substantial L-serine degradation. |