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Hermann Sahm

Researcher at Forschungszentrum Jülich

Publications -  287
Citations -  18348

Hermann Sahm is an academic researcher from Forschungszentrum Jülich. The author has contributed to research in topics: Corynebacterium glutamicum & Zymomonas mobilis. The author has an hindex of 79, co-authored 287 publications receiving 17679 citations.

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Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon.

TL;DR: The amounts of the ilvBNC and ilvNC transcripts increased in response to the addition of alpha-ketobutyrate to the growth medium, correlated to an increase in specific AHAS activity, whereas IR activity was not increased because of the relatively large amount of theIlvC transcript present under all conditions assayed.
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Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-d-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol

TL;DR: It is shown that an open reading frame at 9 min on the chromosomal map of E. coli encodes an enzyme (deoxyxylulose-5-phosphate synthase, DXP synthase) that catalyzes a thiamin diphosphate-dependent acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-ph phosphate to yield DXP.
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Glyceraldehyde 3-Phosphate and Pyruvate as Precursors of Isoprenic Units in an Alternative Non-mevalonate Pathway for Terpenoid Biosynthesis

TL;DR: Incorporation of 13C-labeled glycerol or pyruvate into the ubiquinone Q8 of Escherichia coli mutants lacking enzymes of the triose phosphate metabolism and of (U-13C6)glucose into the triterpenoids of the hopane series of Zymomonas mobilis showed that glyceraldehyde 3-phosphate and a C2 unit derived from pyruVate decarboxylation were the
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Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii.

TL;DR: Evidence is presented which demonstrates that the reaction product of the formaldehyde-dehydrogenase-catalyzed oxidation of formaldehyde is S-formylglutathione rather than formate.