A New Double Coupling System: Synthesis of Citronellyl Acetate via Transacetylation to Citronellol from Acetyl Coenzyme A Produced from Glucose and Free Fatty Acids

2001 ◽  
Vol 65 (8) ◽  
pp. 1917-1919 ◽  
Author(s):  
Shinobu ODA ◽  
Hiromichi OHTA
Keyword(s):  
Fatty Acids ◽  
Free Fatty Acids ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
System Synthesis ◽  
Acetyl Coenzyme ◽  
Citronellyl Acetate ◽  
Coupling System ◽  
Double Coupling

scholarly journals Role of Carnitine Acetyltransferases in Acetyl Coenzyme A Metabolism in Aspergillus nidulans

2011 ◽  
Vol 10 (4) ◽  
pp. 547-555 ◽  
Author(s):  
Michael J. Hynes ◽  
Sandra L. Murray ◽  
Alex Andrianopoulos ◽  
Meryl A. Davis
Keyword(s):  
Fatty Acids ◽  
Aspergillus Nidulans ◽  
Intracellular Transport ◽  
Coenzyme A ◽  
Tricarboxylic Acid Cycle ◽  
Essential Feature ◽  
Malate Synthase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACTThe flow of carbon metabolites between cellular compartments is an essential feature of fungal metabolism. During growth on ethanol, acetate, or fatty acids, acetyl units must enter the mitochondrion for metabolism via the tricarboxylic acid cycle, and acetyl coenzyme A (acetyl-CoA) in the cytoplasm is essential for the biosynthetic reactions and for protein acetylation. Acetyl-CoA is produced in the cytoplasm by acetyl-CoA synthetase during growth on acetate and ethanol while β-oxidation of fatty acids generates acetyl-CoA in peroxisomes. The acetyl-carnitine shuttle in which acetyl-CoA is reversibly converted to acetyl-carnitine by carnitine acetyltransferase (CAT) enzymes is important for intracellular transport of acetyl units. In the filamentous ascomyceteAspergillus nidulans, a cytoplasmic CAT, encoded byfacC, is essential for growth on sources of cytoplasmic acetyl-CoA while a second CAT, encoded by theacuJgene, is essential for growth on fatty acids as well as acetate. We have shown that AcuJ contains an N-terminal mitochondrial targeting sequence and a C-terminal peroxisomal targeting sequence (PTS) and is localized to both peroxisomes and mitochondria, independent of the carbon source. Mislocalization of AcuJ to the cytoplasm does not result in loss of growth on acetate but prevents growth on fatty acids. Therefore, while mitochondrial AcuJ is essential for the transfer of acetyl units to mitochondria, peroxisomal localization is required only for transfer from peroxisomes to mitochondria. Peroxisomal AcuJ was not required for the import of acetyl-CoA into peroxisomes for conversion to malate by malate synthase (MLS), and export of acetyl-CoA from peroxisomes to the cytoplasm was found to be independent of FacC when MLS was mislocalized to the cytoplasm.

scholarly journals Role of Acetyl Coenzyme A Synthesis and Breakdown in Alternative Carbon Source Utilization in Candida albicans

2008 ◽  
Vol 7 (10) ◽  
pp. 1733-1741 ◽  
Author(s):  
Aaron J. Carman ◽  
Slavena Vylkova ◽  
Michael C. Lorenz
Keyword(s):  
Fatty Acids ◽  
Candida Albicans ◽  
Coenzyme A ◽  
Glyoxylate Cycle ◽  
Functional Divergence ◽  
Carbon Sources ◽  
Growth Defect ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACT Acetyl coenzyme A (acetyl-CoA) is the central intermediate of the pathways required to metabolize nonfermentable carbon sources. Three such pathways, i.e., gluconeogenesis, the glyoxylate cycle, and β-oxidation, are required for full virulence in the fungal pathogen Candida albicans. These processes are compartmentalized in the cytosol, mitochondria, and peroxosomes, necessitating transport of intermediates across intracellular membranes. Acetyl-CoA is trafficked in the form of acetate by the carnitine shuttle, and we hypothesized that the enzymes that convert acetyl-CoA to/from acetate, i.e., acetyl-CoA hydrolase (ACH1) and acetyl-CoA synthetase (ACS1 and ACS2), would regulate alternative carbon utilization and virulence. We show that C. albicans strains depleted for ACS2 are unviable in the presence of most carbon sources, including glucose, acetate, and ethanol; these strains metabolize only fatty acids and glycerol, a substantially more severe phenotype than that of Saccharomyces cerevisiae acs2 mutants. In contrast, deletion of ACS1 confers no phenotype, though it is highly induced in the presence of fatty acids, perhaps explaining why acs2 mutants can utilize fatty acids. Strains lacking ACH1 have a mild growth defect on some carbon sources but are fully virulent in a mouse model of disseminated candidiasis. Both ACH1 and ACS2 complement mutations in their S. cerevisiae homolog. Together, these results show that acetyl-CoA metabolism and transport are critical for growth of C. albicans on a wide variety of nutrients. Furthermore, the phenotypic differences between mutations in these highly conserved genes in S. cerevisiae and C. albicans support recent findings that significant functional divergence exists even in fundamental metabolic pathways between these related yeasts.

Effect of Sethoxydim and Haloxyfop on Acetyl-Coenzyme a Carboxylase Activity inFestucaSpecies

Weed Science ◽  
1989 ◽  
Vol 37 (4) ◽  
pp. 512-516 ◽  
Author(s):  
David E. Stoltenberg ◽  
John W. Gronwald ◽  
Donald L. Wyse ◽  
James D. Burton ◽  
David A. Somers ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Tall Fescue ◽  
Coenzyme A ◽  
Carboxylase Activity ◽  
Acetyl Coenzyme A ◽  
Red Fescue ◽  
Acetyl Coenzyme ◽  
Cell Extracts ◽  
Site Of Action ◽  
Acetyl Coenzyme A Carboxylase

In greenhouse studies, the calculated I50(herbicide application resulting in 50% inhibition of shoot regrowth) in tall fescue was approximately 0.004 kg/ha for both sethoxydim and haloxyfop. In red fescue, the I50for sethoxydim and haloxyfop was 9.4 kg/ha and 0.04 kg/ha, respectively. As measured in crude cell extracts of tall fescue, incorporation of14C-acetyl-coenzyme A into fatty acids was inhibited 62 and 71% by 10 μM sethoxydim and 10 μM haloxyfop, respectively. In red fescue, 10 μM haloxyfop inhibited14C-acetyl-CoA incorporation into fatty acids by 29%, whereas 10 μM sethoxydim had no effect. The I50for inhibition of acetyl-coenzyme A carboxylase activity in tall fescue with sethoxydim and haloxyfop was 6.9 and 5.8 μM, respectively. In red fescue the I50for haloxyfop was 118 μM. Sethoxydim concentrations as high as 1 mM had little effect on acetyl-coenzyme A carboxylase activity in red fescue. These results suggest that acetyl-coenzyme A carboxylase is a sensitive site of action for sethoxydim and haloxyfop in tall fescue, and that tolerance to these herbicides in red fescue is due to the presence of a more tolerant form of the enzyme.

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