A link between primary and secondary metabolism: malonyl-CoA formation in Streptomyces ambofaciens growing on ammonium ions or valine

Laakel, Mohamed; Lebrihi, Ahmed; Khaoua, Saïda; Schneider, F.; Lefèbvre, G.; Germain, Pierre

doi:10.1099/00221287-140-6-1451

Cited by 11 publications

(9 citation statements)

References 10 publications

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“…This is consistent with a drain of acetylCoA (an intermediate in methylenomycin synthesis) from the Embden Meyerhoff Parnas pathway. Similar observations were made with respect to the synthesis of spiramycin by S. ambofaciens, in which pyruvate is drained from the Embden Meyerhoff Parnas pathway to yield, in that case, malonyl-CoA (Laakel et al, 1994). The flux analysis of S. coelicolor presented by Naeimpoor and Mavituna (2000) cannot be readily compared to the results presented here.…”

Section: Discussionsupporting

confidence: 75%

Carbon Flux Distribution in Antibiotic-Producing Chemostat Cultures of Streptomyces lividans

Rossa

White

Kuiper

et al. 2002

Metabolic Engineering

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Section: Discussionsupporting

confidence: 75%

Carbon Flux Distribution in Antibiotic-Producing Chemostat Cultures of Streptomyces lividans

Rossa

White

Kuiper

et al. 2002

Metabolic Engineering

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“…Three sugars, mycaminose, forosamine and mycarose, are linked to the lactone ring to form the macrolide [7]. Improvement of spiramycin production [8] and its regulation by phosphate [9,10], carbon [11][12][13] and nitrogen sources [14][15][16][17][18] has been investigated as well as genetic aspects [19][20][21].…”

Section: Introductionmentioning

confidence: 99%

Effects of glucose limitation on biomass and spiramycin production by Streptomyces ambofaciens

Colombié

Bideaux

Goma

et al. 2005

Bioprocess Biosyst Eng

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Spiramycin production by Streptomyces ambofaciens Sp181110 with glucose as the carbon source was studied under a controlled nutritional environment. In a batch culture, the glucose excess after ammonium depletion led to pyruvate and alpha-ketoglutarate accumulation. 85 mg/l of spiramycin were produced in less than 70 h during the stationary and maintenance phase on these acids after glucose exhaustion. Fed-batch strategy was designed to study spiramycin production without by-product formation and glucose accumulation. In these conditions, up to 150 mg/l were produced in less than 80 h during the stationary phase on glucose. The antibiotic titre was found independent of the glucose feeding under carbon limitation and the importance of putative intracellular reserves formed after nutrient exhaustion was suggested. Besides, spiramycin production was not inhibited by the limiting flux of glucose.

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“…Attempts to purify a complex with acetyl-CoA carboxylase activity from streptomycetes have been unsuccessful, probably reflecting its high instability in vitro (7). An alternative pathway for the biosynthesis of malonyl-CoA was described in Streptomyces aureofaciens (2,25) and involved the anaplerotic enzymes phosphoenolpyruvate carboxylase and oxaloacetate dehydrogenase. However, oxaloacetate dehydrogenase could not be detected in S. coelicolor A3(2) (6), where malonyl-CoA synthesis appears to occur exclusively through the acetyl-CoA carboxylase complex.…”

mentioning

confidence: 99%

Role of an Essential Acyl Coenzyme A Carboxylase in the Primary and Secondary Metabolism of Streptomyces coelicolor A3(2)

Rodrı́guez

Banchio

Diacovich

et al. 2001

Appl Environ Microbiol

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Two genes, accB and accE, that form part of the same operon, were cloned from Streptomyces coelicolor A3(2). AccB is homologous to the carboxyl transferase domain of several propionyl coezyme A (CoA) carboxylases and acyl-CoA carboxylases (ACCases) of actinomycete origin, while AccE shows no significant homology to any known protein. Expression of accB and accE in Escherichia coli and subsequent in vitro reconstitution of enzyme activity in the presence of the biotinylated protein AccA1 or AccA2 confirmed that AccB was the carboxyl transferase subunit of an ACCase. The additional presence of AccE considerably enhanced the activity of the enzyme complex, suggesting that this small polypeptide is a functional component of the ACCase. The impossibility of obtaining an accB null mutant and the thiostrepton growth dependency of a tipAp accB conditional mutant confirmed that AccB is essential for S. coelicolor viability. Normal growth phenotype in the absence of the inducer was restored in the conditional mutant by the addition of exogenous long-chain fatty acids in the medium, indicating that the inducer-dependent phenotype was specifically related to a conditional block in fatty acid biosynthesis. Thus, AccB, together with AccA2, which is also an essential protein (E. Rodriguez and H. Gramajo, Microbiology 143:3109-3119, 1999), are the most likely components of an ACCase whose main physiological role is the synthesis of malonyl-CoA, the first committed step of fatty acid synthesis. Although normal growth of the conditional mutant was restored by fatty acids, the cultures did not produce actinorhodin or undecylprodigiosin, suggesting a direct participation of this enzyme complex in the supply of malonyl-CoA for the synthesis of these secondary metabolites.

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A link between primary and secondary metabolism: malonyl-CoA formation in Streptomyces ambofaciens growing on ammonium ions or valine

Cited by 11 publications

References 10 publications

Carbon Flux Distribution in Antibiotic-Producing Chemostat Cultures of Streptomyces lividans

Carbon Flux Distribution in Antibiotic-Producing Chemostat Cultures of Streptomyces lividans

Effects of glucose limitation on biomass and spiramycin production by Streptomyces ambofaciens

Role of an Essential Acyl Coenzyme A Carboxylase in the Primary and Secondary Metabolism of Streptomyces coelicolor A3(2)

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