Journal
JOURNAL OF BACTERIOLOGY
Volume 184, Issue 6, Pages 1750-1758Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.184.6.1750-1758.2002
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R43GM039646] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM98933, GM39646] Funding Source: Medline
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Most serine cycle methylotrophic bacteria lack isocitrate lyase and convert acetyl coenzyme A (acetyl-CoA) to glyoxylate via a novel pathway thought to involve butyryl-CoA and propionyl-CoA as intermediates. In this study we have used a genome analysis approach followed by mutation to test a number of genes for involvement in this novel pathway. We show that methylmalonyl-CoA mutase, an R-specific crotonase, isobutyryl-CoA dehydrogenase, and a GTPase are involved in glyoxylate regeneration. We also monitored the fate of C-14- labeled carbon originating from acetate, butyrate, or bicarbonate in mutants defective in glyoxylate regeneration and identified new potential intermediates in the pathway: ethylmalonyl-CoA, methylsuccinyl-CoA, isobutyryl-CoA, methacrylyl-CoA, and beta-hydroxyisobutyryl-CoA. A new scheme for the pathway is proposed based on these data.
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