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At least 19 recordsLinked to original sources
PubMed1989

The "survival hormones": azelaic and pimelic acids, suppress the stress elicited by isolation conditions on the steroids and phospholipids of adult worker honeybees.

The kinetics of abdomen, haemolymph and thoracic-muscle steroid and phospholipid concentrations have been determined in adult worker-bees kept for 0 to 12 hrs starving in darkness, either grouped by 8 (controls) or strictly isolated, or isolated in presence of a piece of cotton impregnated with 1 microgram azelaic acid and 1 microgram pimelic acid, the so-called "survivones" which restore the lifespan of isolated bees. The dynamics of both steroids and phospholipids strongly deviates in isolated bees relatively to controls. The introduction of survivones completely restored the variations of haemolymph steroids of haemolymph and thorax phospholipids of isolated bees to exactly similar features as in controls. The action of the lipoic hormones "survivones" thus involves the participation of lipid metabolism.

Abdomen↗
PubMed1988

Formation of a biotin precursor, pimelic acid, in yeasts from C18 fatty acids.

The biosynthesis of biotin-vitamers from C18 fatty acids in the resting cell reaction system of yeasts was investigated. The formation of pimelic acid (a biotin precursor) and biotin-vitamers (a mixture of 7-keto-8-aminopelargonic acid and dethiobiotin) from linolenic, linoleic, and oleic acids was observed in certain yeasts belonging to the genera Cryptococcus, Candida, Rhodotorula, and Trichosporon. Metabolites from linolenic acid were analyzed by gas-liquid chromatography and mass spectrometry. Linoleic, oleic, stearic, heptadecanoic, palmitic, pentadecanoic, and pimelic acids were identified as metabolites of linolenic acid. The existence of a route to pimelic acid from linolenic acid in a strain of Rhodotorula rubra AKU 4836 was also indicated.

Candida↗
PubMed1992

Azelaic and pimelic acids: metabolic intermediates or artefacts?

Azelaic and pimelic acids are excreted in elevated amounts in urine in disorders of mitochondrial beta-oxidation and disorders of peroxisomal beta-oxidation, for which they are of significant diagnostic value. We have detected the presence of azelaic, pimelic and even-chain-length dicarboxylic acids (adipic, suberic and sebacic acids) arising artefactually as a result of storage of small sample volumes in plastic containers. Storage of samples for organic acid analysis in glass containers is recommended.

Adipates↗
PubMed1979

Pattern of aliphatic dicarboxylic acids in uremic serum including a new organic acid, 2,4-dimethyladipic acid.

(1) 2,4-Dimethyladipic acid was first identified in normal human urine using gas chromatography-mass spectrometry. Urinary excretion of 2,4-dimethyladipic acid in 7 healthy adults ranged from 4.9 mumol to 14 mumol per 24 h. (2) Succinic acid, adipic acid, 3-methyladipic acid, 2,4-dimethyladipic acid, pimelic acid and azelaic acid were identified in the ultrafiltrate of the blood obtained from a chronic uremic patient using a hemodialyzer. (3) Levels of succinic acid, adipic acid, 3-methyladipic acid, 2,4-dimethyladipic acid, pimelic acid and azelaic acid in uremic serum were determined using a mass fragmentographic technique. Concentration of succinic acid in uremic serum was comparable to that in normal serum, whereas concentrations of adipic acid, 3-methyladipic acid, 2,4-dimethyladipic acid, pimelic acid and azelaic acid were highly elevated in uremic serum.

Adipates↗
PubMed1976

Anaerobic degradation of benzoate to methane by a microbial consortium.

A stabilized consortium of microbes which anaerobically degraded benzoate and produced CH4 was established by inoculation of a benzoate-mineral salts medium with sewage sludge; the consortium was routinely subcultured anaerobically in this medium for 3 years. Acetate, formate, H2 and CO2 were identified as intermediates in the overall conversion of benzoate to CH4 by the culture. Radioactivity was equally divided between the CH4 and CO2 from the degradation of uniformly ring-labeled [14C]benzoate. The methyl group of acetate was stoichiometrically converted to CH4. Acetate, cyclohexanecarboxylate, 2-hydroxycyclohexanecarboxylate, o-hydroxybenzoic acid and pimelic acid were converted to CH4 without a lag suggesting that benzoate was degraded by a reductive pathway. Addition of o-chlorobenzoate inhibited benzoate degradation but not acetate degradation or methane formation. Two methanogenic organisms were isolated from the mixed culture; neither organism was able to degrade benzoate, showing that the methanogenic bacteria served as terminal organisms of a metabolic food chain composed of several organisms. Removal of intermediates by the methanogenic bacteria provided thermodynamically favorable conditions for benzoate degradation.

Acetates↗
PubMed1975

Biological studies of amiclenomycin.

The action of amiclenomycin (AM) in inhibiting growth of microorganisms is specific against mycobacteria in vitro, but the antibiotic does not show a therapeutic effect against tubercle bacilli in vivo. The action of AM is reversed by biotin, desthiobiotin (DTB) and 7,8-diaminopelargonic acid (DAPA), but not by 7-keto-8-aminopelargonic acid (KAPA), pimelic acid and glutaric acid. In the presence of AM, cultures of Mycobacterium smegmatis and Bacillus sphaericus accumulated KAPA, whereas the formation of DTB decreased. Therefore, AM is thought to inhibit KAPA-DAPA transamination in biotin biosynthesis. In M. smegmatic and B. sphaericus the conversions of KAPA to DAPA and of DTB to biotin were rate limiting in biotin synthesis. Accordingly, the synergistic antibiotic activity of AM, inhibiting the former, and actithiazic acid, inhibiting the latter reaction, would be simply explained.

Amino Acids, Diamino↗
PubMed1991

Metabolism of deuterium-labeled nonanoic acids in the riboflavin-deficient rat model of multiple acyl-CoA dehydrogenase deficiency.

Riboflavin-deficient rats are used to study the metabolism of deuterium-labeled nonanoic acids under conditions mimicking the human disorder of multiple acyl-CoA dehydrogenase deficiency in which large amounts of ethyl-malonic, glutaric, adipic, suberic, 4-octenedioic, sebacic and 4-decenedioic acids are excreted. Both control and deficient rats convert the nonanoic acids to labeled azelaic and pimelic acids. The labeling pattern in pimelic acid is consistent with the omega-oxidation of nonanoic acids to azelaic acid followed by beta-oxidation to pimelic acid.

Acyl-CoA Dehydrogenases↗
PubMed1977

Action of 5-(2-thienyl)valeric acid as a biotin antagonist.

5-(2-Thienyl)valeric acid (TVA), a biotin analogue which can be easily prepared through chemical process, inhibited the growth of a biotin synthesizing Rhodotorula glutinis. The growth inhibition was reversed by the addition of biotin. Among biotin intermediates, dethiobiotin and 7,8-diaminopelargonic acid reversed the inhibition by TVA, while 7-keto-8-amino-pelargonic acid and pimelic acid did not. From these results, it was concluded that TVA is a biotin antagonist which probably acts as an inhibitor of biotin biosynthesis.

Biotin↗
PubMed1975

Physiological function of the Pseudomonas putida PpG6 (Pseudomonas oleovorans) alkane hydroxylase: monoterminal oxidation of alkanes and fatty acids.

Pseudomonas putida PpG6 is able to utilize purified n-alkanes of six to ten carbon atoms for growth. It can also grow on the primary terminal oxidation products of these alkanes and on 1-dodecanol but not on the corresponding 2-ketones or 1,6-hexanediol, adipic acid, or pimelic acid. Revertible point mutants can be isolated which have simultaneously lost the ability to grow on all five n-alkane growth substrates but which can still grow on octanol or nonanol. An acetate-negative mutant defective in isocitrate lysase activity is unable to grow on even-numbered alkanes and fatty acids. Analysis of double mutants defective in acetate and propionate or in acetate and glutarate metabolism shows that alkane carbon is assimilated only via acetyl-coenzyme A and propionyl-coenzyme A. These results support the following conclusions: (i) The n-alkane growth specificity of P. putida PpG6 is due to the substrate specificity of whole-cell alkane hydroxylation; (ii) there is a single alkane hydroxylase enzyme complex; (iii) the physiological role of this complex is to initiate the monoterminal oxidation of alkane chains; and (iv) straight-chain fatty acids from butyric through nonanoic are degraded exclusively by beta-oxidation from the carboxyl end of the molecule.

Alkanes↗
PubMed1990

[10-Acyldithranol dimers; new derivatives of the antipsoriatic dithranol; synthesis, characterization and biochemical properties].

With regard to the synthesis of 10-(omega-carboxyacyl)-derivatives dithranol 1 was reacted with the carboxylic acid dichlorides of succinic acid, glutaric acid, adipic acid and pimelic acid in toluene and collidin as a base. Instead of the expected derivatives the 10-acyldithranol dimers 5-7 were isolated as main products except for the reaction of succinyl chloride where only lactone 2 was formed. Moreover the 6-ring lactone 3 as a side product and traces of the 7-ring lactone 4 could also be isolated and characterized. All compounds revealed to be inhibitors of the enzyme glucose-6-phosphate dehydrogenase, indicating antipsoriatic activity.

Anthralin↗
PubMed1999

Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35.

A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia coli to yield an active enzyme. The purified enzyme had a pH optimum of approximately 8.0, Km values of 0.49 mM for pimelic acid, 0.18 mM for CoA and 0.72 mM for ATP, a subunit Mr of approximately 80000 as determined by SDS/PAGE, and was found to be a tetramer by gel-filtration chromatography. The specific activity of the purified enzyme was 77.3 units/mg of protein. The enzyme was not absolutely specific for pimelic acid. The relative activity for adipic acid (C6) was 72% and for azaleic acid (C9) was 18% of that for pimelic acid (C7). The N-terminal amino acid was blocked to amino acid sequencing, but controlled proteolysis resulted in three peptide fragments for which amino acid sequences were obtained. An oligonucleotide gene probe corresponding to one of the amino acid sequences was synthesized and used to isolate the gene (pauA, pimelic acid-utilizing A) coding for pimeloyl-CoA synthetase. The pauA gene, which codes for a protein with a theoretical Mr of 74643, was then sequenced. The deduced amino acid sequence of the enzyme showed similarity to hypothetical proteins from Archaeoglobus fulgidus, Methanococcus jannaschii, Pyrococcus horikoshii, E. coli and Streptomyces coelicolor, and some limited similarity to microbial succinyl-CoA synthetases. The similarity with the protein from A. fulgidus was especially strong, thus indicating a function for this unidentified protein. The pauA gene was cloned into E. coli, where it was expressed and resulted in an active enzyme.

Acyl Coenzyme A↗
PubMed1993

Biotin biosynthesis in higher plant cells. Identification of intermediates.

Biotin biosynthesis was investigated in lavender cell cultures (Lavandula vera L.). Two different biological assays and two different HPLC procedures were used to identify all the intermediates involved in biotin biosynthesis. The pathway for biotin biosynthesis could be analyzed starting with [3H]pimelic acid as precursor, leading to labelled biotin and even to labelled biotinylated enzymes. Intermediates known from the bacterial pathway (7-oxo-8-amino-pelargonic acid, 7,8-diamino-pelargonic acid, dethiobiotin) were present in detectable amounts. Pimelic acid activation to pimeloyl-CoA could be observed. In contrast to bacterial cells, an unknown stable labelled intermediate, named compound A, accumulated. This compound coeluted with an authentic sample of 9-mercaptodethiobiotin from HPLC with an anion-exchange column and was as effective as biotin in supporting the growth of the strain bioB105 of Escherichia coli. When 3H-labelled compound A was added to the growth medium of the lavender cells it was incorporated in an acidomycin-sensitive manner into biotin. [3H]Dethiobiotin was incorporated into both compound A and biotin. These results strongly suggest that, in higher plant cells, the reaction catalysed by biotin synthase may proceed in two distinct steps involving mercaptodethiobiotin (9-mercaptodethiobiotin?) as an intermediate.

Acyl Coenzyme A↗