Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum

Merkamm, Muriel; Chassagnole, Christophe; Lindley, Nic D.; Guyonvarch, Armel

doi:10.1016/s0168-1656(03)00145-7

Cited by 39 publications

(36 citation statements)

References 20 publications

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“…Still, glucose feeding, aeration, pH, and the medium components appeared to play important roles in controlling the yield of valine. Further genetic engineering involving ilvA knockout, ilvD introduction, and panBC knockouts seem to be useful for more efficient valine production, as reported previously 27,28) and might be applicable in combination with our results (Fig. 1).…”

Section: Discussionsupporting

confidence: 80%

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

Wada

Hijikata

Aoki

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionsupporting

confidence: 80%

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

Wada

Hijikata

Aoki

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…The acetohydroxy acid isomerase, IlvC, has also been shown to function as a KPR in E. coli and S. Typhimurium, converting 2-dehydropantoate to pantoate, similar to PanE (5,6). In some species, e.g., Corynebacterium glutamicum, IlvC is the sole KPR (7). In the final step of the pantothenate synthesis pathway, pantoate and ␤-alanine are ligated by the pantothenate synthase, PanC, to form pantothenate (8).…”

mentioning

confidence: 99%

PanG, a New Ketopantoate Reductase Involved in Pantothenate Synthesis

Miller

LoVullo

Kijek

et al. 2012

Journal of Bacteriology

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Pantothenate, commonly referred to as vitamin B 5 , is an essential molecule in the metabolism of living organisms and forms the core of coenzyme A. Unlike humans, some bacteria and plants are capable of de novo biosynthesis of pantothenate, making this pathway a potential target for drug development. Francisella tularensis subsp. tularensis Schu S4 is a zoonotic bacterial pathogen that is able to synthesize pantothenate but is lacking the known ketopantoate reductase (KPR) genes, panE and ilvC, found in the canonical Escherichia coli pathway. Described herein is a gene encoding a novel KPR, for which we propose the name panG (FTT1388), which is conserved in all sequenced Francisella species and is the sole KPR in Schu S4. Homologs of this KPR are present in other pathogenic bacteria such as Enterococcus faecalis, Coxiella burnetii, and Clostridium difficile. Both the homologous gene from E. faecalis V583 (EF1861) and E. coli panE functionally complemented Francisella novicida lacking any KPR. Furthermore, panG from F. novicida can complement an E. coli KPR double mutant. A Schu S4 ⌬panG strain is a pantothenate auxotroph and was genetically and chemically complemented with panG in trans or with the addition of pantolactone. There was no virulence defect in the Schu S4 ⌬panG strain compared to the wild type in a mouse model of pneumonic tularemia. In summary, we characterized the pantothenate pathway in Francisella novicida and F. tularensis and identified an unknown and previously uncharacterized KPR that can convert 2-dehydropantoate to pantoate, PanG.

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“…In C. glutamicum, the ilvC gene product is the only enzyme capable of producing pantoate (85). Primerano and Burns isolated mutants in α-ketopantoate reductase and clarified the relationship between pantoate and branched-chain amino acid biosynthesis in S. typhimurium (101,102).…”

Section: Pantoate Biosynthesismentioning

confidence: 99%

Biosynthesis of Pantothenic Acid and Coenzyme A

Leonardi¹,

Jackowski²

2007

EcoSal

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Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum

Cited by 39 publications

References 20 publications

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

PanG, a New Ketopantoate Reductase Involved in Pantothenate Synthesis

Biosynthesis of Pantothenic Acid and Coenzyme A

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Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum

Cited by 39 publications

References 20 publications

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H+-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H+-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

PanG, a New Ketopantoate Reductase Involved in Pantothenate Synthesis

Biosynthesis of Pantothenic Acid and Coenzyme A

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Product

Resources

About

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase

Enhanced Valine Production inCorynebacterium glutamicumwith Defective H⁺-ATPase and C-Terminal Truncated Acetohydroxyacid Synthase