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@ARTICLE{Bartek:15863,
author = {Bartek, T. and Blombach, B. and Lang, S. and Eikmanns, B.J.
and Wiechert, W. and Oldiges, M. and Nöh, K. and Noack, S.},
title = {{C}omparative 13{C}-metabolic flux analysis of pyruvate
dehydrogenase complex-deficient {L}-valine-producing
{C}orynebacterium glutamicum},
journal = {Applied and environmental microbiology},
volume = {77},
issn = {0099-2240},
address = {Washington, DC [u.a.]},
publisher = {Soc.},
reportid = {PreJuSER-15863},
pages = {6644 - 6652},
year = {2011},
note = {This work was financially supported by the Fachagentur
Nachwachsende Rohstoffe (Agency for Renewable Resources) of
the BMVEL, German Federal Ministry of Food, Agriculture and
Consumer Protection (grant 04NR003/22000304), and by Evonik
Degussa GmbH.},
abstract = {L-Valine can be formed successfully using C. glutamicum
strains missing an active pyruvate dehydrogenase enzyme
complex (PDHC). Wild-type C. glutamicum and four
PDHC-deficient strains were compared by (13)C metabolic flux
analysis, especially focusing on the split ratio between
glycolysis and the pentose phosphate pathway (PPP). Compared
to the wild type, showing a carbon flux of $69\%$ ± $14\%$
through the PPP, a strong increase in the PPP flux was
observed in PDHC-deficient strains with a maximum of $113\%$
± $22\%.$ The shift in the split ratio can be explained by
an increased demand of NADPH for l-valine formation. In
accordance, the introduction of the Escherichia coli
transhydrogenase PntAB, catalyzing the reversible conversion
of NADH to NADPH, into an L-valine-producing C. glutamicum
strain caused the PPP flux to decrease to $57\%$ ± $6\%,$
which is below the wild-type split ratio. Hence,
transhydrogenase activity offers an alternative perspective
for sufficient NADPH supply, which is relevant for most
amino acid production systems. Moreover, as demonstrated for
L-valine, this bypass leads to a significant increase of
product yield due to a concurrent reduction in carbon
dioxide formation via the PPP.},
keywords = {Carbon Dioxide: metabolism / Carbon Isotopes: metabolism /
Corynebacterium glutamicum: genetics / Corynebacterium
glutamicum: metabolism / Escherichia coli: enzymology /
Escherichia coli: genetics / Escherichia coli Proteins:
genetics / Escherichia coli Proteins: metabolism /
Glycolysis / NADP Transhydrogenases: genetics / NADP
Transhydrogenases: metabolism / Pentose Phosphate Pathway /
Pyruvate Dehydrogenase Complex: genetics / Valine:
metabolism / Carbon Isotopes (NLM Chemicals) / Escherichia
coli Proteins (NLM Chemicals) / Pyruvate Dehydrogenase
Complex (NLM Chemicals) / Carbon Dioxide (NLM Chemicals) /
Valine (NLM Chemicals) / NADP Transhydrogenases (NLM
Chemicals) / pntA protein, E coli (NLM Chemicals) / pntB
protein, E coli (NLM Chemicals) / J (WoSType)},
cin = {IBT-2},
ddc = {570},
cid = {I:(DE-Juel1)VDB56},
pnm = {Biotechnologie},
pid = {G:(DE-Juel1)FUEK410},
shelfmark = {Biotechnology $\&$ Applied Microbiology / Microbiology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21784914},
pmc = {pmc:PMC3187166},
UT = {WOS:000294691400040},
doi = {10.1128/AEM.00575-11},
url = {https://juser.fz-juelich.de/record/15863},
}