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PubMed1969

Oxoenoic acids as metabolites in the bacterial degradation of catechols.

1. Partially purified extracts of a Pseudomonas converted the meta ring-fission product of 4-methylcatechol into a compound having spectroscopic and chemical properties consistent with its being 2-oxohex-4-enoic acid. 2. Catechol and 3-methylcatechol were both metabolized to a compound that appeared to be 2-oxopent-4-enoic acid. 3. Solutions of norvaline and norleucine were prepared from these metabolites. 4. A reaction scheme is presented for the conversion of catechols into hydroxyoxo acids after meta ring-fission.

Caproates↗
PubMed1976

Identification of cysteine as the reactive group in pyruvate kinase alkylated by 5-chloro-4-oxopentanoic acid.

4-Hydroxypentanoic acid alanine thioether was synthesized and characterized by n.m.r. spectroscopy. This derivative corresponded to the modified amino acid obtained by allowing 5-chloro-4-oxo[3,5-3H]pentanoic acid to react with rabbit muscle pyruvate kinase. Performic acid oxidation of 4-oxo[3,5-3H]pentanoic acid alanine thioether in pyruvate kinase gave [3H]succinate (67%) and [3H]carboxymethylcysteine (33%) as expected. Evidence is presented to show that NaBH4 reduction followed by periodate oxidation and analysis of radioactive formaldehyde production may provide a convenient method for distinguishing between thiol and amino alkylation by halogenomethyl ketone compounds. Peptide 'mapping' confirms that the modification by 5-chloro-4-oxopentanoic acid occurs primarily at one region of pyruvate kinase.

Alkylation↗
PubMed1975

Morphological alterations and ganglioside sialyltransferase activity induced by small fatty acids in HeLa cells.

Incubation of HeLa cells in the presence of millimolar concentrations of propionate, butyrate, or pentanoate increases the specific activity of CMP-sialic acid:lactosylceramide sialyltransferase 7-20-fold within 24 h. Longer-chain saturated fatty acids or acetate are much less effective, decanoate showing no induction. Unsaturated fatty acid analogs of butyrate and other compounds are ineffective. Only the three most effective compounds also produce characteristic smooth extended cell processes in HeLa cells. Butyrate (5 mM) induces the sialyltransferase after a 4-h lag, producing maximum specific activity by 24 h. The amount of sialyl-lactosylceramide, the glycolipid product of the enzyme, increases during that time 3.5 times more than in control cultures. No other glycosphingolipid enzyme is significantly altered by butyrate exposure. The cellular shape changes occur 2-3 h later than the increase of sialyltransferase activity, and both processes require the continuous presence of inducer and the synthesis of RNA and protein but not the synthesis of DNA or the presence of serum.

Blood Proteins↗
PubMed1978

Nutritional Requirements of Selenomonas ruminantium for Growth on Lactate, Glycerol, or Glucose.

The nutritional requirements of Selenomonas ruminantium HD4 for growth on glucose, glycerol, or lactate were investigated to clarify the results of previous studies and to relate the nutrition of the organism to its physiology. The organism required l-aspartate, CO(2), p-aminobenzoic acid, and biotin for growth on a lactate-salts medium that contained small amounts of dithiothreitol. Aspartate could be replaced by l-malate or fumarate but not by succinate or l-asparagine. Requirements for growth with glycerol as an energy source were similar, except that aspartate was not required. With glucose as the energy source, neither aspartate nor p-aminobenzoic acid was required, but a requirement for volatile fatty acids, which could be met by n-valerate, was observed. CO(2) was required for growth on lactate or glycerol but not on glucose on complex media containing Trypticase and yeast extract. Sulfide could be used as the sole source of sulfur.

Journal Article↗
PubMed1974

D-lysine catabolic pathway in Pseudomonas putida: interrelations with L-lysine catabolism.

The isolation of several mutant strains blocked in l-lysine degradation has permitted an assessment of the physiological significance of enzymatic reactions related to lysine metabolism in Pseudomonas putida. Additional studies with intact cells involved labeling of metabolic intermediates from radioactive l- or d-lysine, and patterns of enzyme induction in both wild-type and mutant strains. These studies lead to the conclusions that from l-lysine, the obligatory pathway is via delta-aminovaleramide, delta-aminovalerate, glutaric semialdehyde, and glutarate, and that no alternative pathways from l-lysine exist in our strain. A distinct pathway from d-lysine proceeds via Delta(1)-piperideine-2-carboxylate, l-pipecolate, and Delta(1)-piperideine-6-carboxylate (alpha-aminoadipic semialdehyde). The two pathways are independent in the sense that certain mutants, unable to grow on l-lysine, grow at wild-type rates of d-lysine, utilizing the same intermediates as the wild type, as inferred from labeling studies. This finding implies that lysine racemase in our strain, while detectable in cell extracts, is not physiologically functional in intact cells at a rate that would permit growth of mutants blocked in the l-lysine pathway. Pipecolate oxidase, a d-lysine-related enzyme, is induced by d-lysine and less efficiently by l-lysine. Aminooxyacetate virtually abolishes the inducing activity of l-lysine for this enzyme, suggesting that lysine racemase, although functionally inactive for growth purposes, may still have regulatory significance in permitting cross-induction of d-lysine-related enzymes by l-lysine, and vice versa. This finding suggests a mechanism in bacteria for maintaining regulatory patterns in pathways that may have lost their capacity to support growth. In addition, enzymatic studies are reported which implicate Delta(1)-piperideine-2-carboxylate reductase as an early step in the d-lysine pathway.

Acetates↗
PubMed1974

Distribution of the isopropylmalate pathway to leucine among diverse bacteria.

alpha-Isopropylmalate synthase and beta-isopropylmalate dehydrogenase activities were detected in extracts of the following organisms: Chromatium D, Rhodopseudomonas spheroides, Hydrogenomonas H16, Pseudomonas aeruginosa, Pseudomonas fluorescens, Vibrio extorquens, Rhizobium japonicum, Alcaligenes viscolactis, Escherichia coli B, Proteus vulgaris, Aerobacter aerogenes, Salmonella typhimurium, Micrococcus sp., Micrococcus lysodeikticus, Bacillus polymyxa, Bacillus subtilis, and Nocardia opaca. The alpha-isopropylmalate synthase activity in these extracts was inhibited by low concentrations of l-leucine. Taken together with other data, these results suggest that the isopropylmalate pathway is widespread among organisms that can synthesize leucine.

Alcohol Oxidoreductases↗
PubMed1976

Mutants of Saccharomycopsis lipolytica defective in lysine catabolism.

Wild-type strains of Saccharomycopsis lipolytica are able to use lysine as a carbon or a nitrogen source, but not as a unique source for both. Mutants were selected that could not use lysine either as a nitrogen or as a carbon source. Some of them, however, utilized N-6-acetyllysine or 5-aminovaleric acid. Many of the mutants appeared to be blocked in both utilizations, suggesting a unique pathway for lysine degradation (either as a carbon or as a nitrogen source). Genetic characterization of these mutants was achieved by complementation and recombination tests.

2-Aminoadipic Acid↗
PubMed2005

Multiple and interconnected pathways for L-lysine catabolism in Pseudomonas putida KT2440.

L-lysine catabolism in Pseudomonas putida KT2440 was generally thought to occur via the aminovalerate pathway. In this study we demonstrate the operation of the alternative aminoadipate pathway with the intermediates D-lysine, L-pipecolate, and aminoadipate. The simultaneous operation of both pathways for the use of L-lysine as the sole carbon and nitrogen source was confirmed genetically. Mutants with mutations in either pathway failed to use L-lysine as the sole carbon and nitrogen source, although they still used L-lysine as the nitrogen source, albeit at reduced growth rates. New genes were identified in both pathways, including the davB and davA genes that encode the enzymes involved in the oxidation of L-lysine to delta-aminovaleramide and the hydrolysis of the latter to delta-aminovalerate, respectively. The amaA, dkpA, and amaB genes, in contrast, encode proteins involved in the transformation of Delta1-piperidine-2-carboxylate into aminoadipate. Based on L-[U-13C, U-15N]lysine experiments, we quantified the relative use of pathways in the wild type and its isogenic mutants. The fate of 13C label of L-lysine indicates that in addition to the existing connection between the D- and L-lysine pathways at the early steps of the catabolism of L-lysine mediated by a lysine racemase, there is yet another interconnection at the lower end of the pathways in which aminoadipate is channeled to yield glutarate. This study establishes an unequivocal relationship between gene and pathway enzymes in the metabolism of L-lysine, which is of crucial importance for the successful colonization of the rhizosphere of plants by this microorganism.

2-Aminoadipic Acid↗
PubMed1990

Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts.

Isovaleric acidemia (IVA) is caused by a genetic deficiency of isovaleryl-CoA dehydrogenase (IVD). At least five distinct variant IVD alleles are known. We isolated five overlapping IVD cDNA clones from a human placenta cDNA library. They covered the entire coding region, except the initiation codon, and 587 bp in the 3'-noncoding region plus the poly(A) tail. The structure of the initiation site was identified by the study of genomic DNA and by the sequence comparison with rat IVD. Human IVD shared 89.6, 35.8, and 31.6% identical amino acid residues with rat IVD and human short and medium chain acyl-CoA dehydrogenases, respectively. In the Northern blot analysis of normal human liver and fibroblast poly(A)+ RNA, three mRNA species of different sizes (4.6, 3.8, and 2.1 kb) hybridized to IVD cDNA. Three mRNA species with similar sizes were also detected in five IVA fibroblast lines of different genotypes (variants 1, 1 X 2, 2, 3, and 5), suggesting that these variants are each due to a point mutation or small deletion.

Amino Acid Sequence↗
PubMed1981

Propionyl-CoA carboxylase deficiency: case report, effect of low-protein diet and identification of 3-oxo-2-methylvaleric acid 3-hydroxy-2-methylvaleric acid, and maleic acid in urine.

Vomiting, lethargy and metabolic acidosis were the main initial symptoms of metabolic disease in a 1 month old girl. Her older sister had died from a similar disease, considered to be Reye's syndrome, at an age of 15 months. The urine of the present case contained 2-methylcitric acid, 3-hydroxypropionic acid, N-propionylglycine, 2-hydroxy-3-methylbutyric acid, N-tiglylglycine, 3-hydroxyvaleric acid and glutaric acid. These metabolites are all known to be associated with propionyl-CoA accumulation. Free propionic acid was not detected in the urine. In addition, the urine contained 3-oxo-2-methylvaleric acid and 3-hydroxy-2-methylvaleric acid, probably formed by condensation of two molecules of propionyl-CoA. The identity of these metabolites was confirmed by synthesis. An elevated urinary concentration of maleic acid and fumaric acid was another constant abnormality. The activity of propionyl-CoA carboxylase in leucocytes was about 20% of the normal activity. The girl was teated with a low-protein diet since the diagnosis was made at an age of 1 month, and her psychomotor development was satisfactory at an age of 2 1/2 years. She had a few episodes of acidosis during infections.

Amino Acid Metabolism, Inborn Errors↗
PubMedDate not supplied

[Effect of 2-phenyl-3-methyl-3-hydroxypentanoic and 2,3-diphenyl-3-hydroxypentanoic acids on the lipolytic activity of rat adipose tissue].

Aromatic derivatives of mevalonic acid (2-phenyl-3-methyl-3-hydroxy pentanic and 2,3-diphenyl-3-hydroxy pentanic acids) decreased the yield of unesterified fatty acids from adipose tissue by about 28-36 percent after subcutaneous administration into rats within one or two weeks and under conditions of incubation of the adipose tissue in vitro. Distinct decrease in the yield of glycerol was cause by 2,3-diphenyl-3-hydroxy pentanic acid (1 with 10-minus 3 = 5 with 10-minus 3 M) under conditions of lipolysis stimulated by adrenaline. Antilipolytic effect of the preparation was more pronounced than that of well-known hypolipidemic drug clofibrate (p-chlorophenhydroxy isobutyrate).

Adipose Tissue↗
PubMed1979

[Emergency treatment of inborn amino errors of amino acid metabolism detected in the neonatal period].

The indications and effects of exchange transfusion, peritoneal dialysis, osmotic diuresis and early feeding have been studied in 28 children with inborn errors of aminoacid metabolism presenting in the neonatal period. Exchange-transfusion has only a transitory and incomplete effect but it is simple and quick. Peritoneal dialysis has a remarkable and often life-saving effect because the blood levels of toxic metabolites are reduced very effectively in organic acidaemias. However the rate of removal may decline if plasma concentrations fall below a critical level (1.2 mmol/L foor leucine). If the dialysis is prolonged for more than 36 hours it may cause hypoprotidaemia. Osmotic diuresis increases the 45 ml/min. However it is of little elimination of methylmalonic acid because the renal clearance is between 15 and 45 ml/min. However it is of little value in maple syrup urine disease, propionic acidaemia or isovaleric acidaemia because the renal clearance of the toxic metabolites is so low. The early re-introduction of low protein high calorie of a low protein and high calorie diet by continuous intragastric feeding is very important. The authors propose a protocol for the treatment of babies presenting inborn errors of aminoacid metabolism in the neonatal period. Peritoneal dialysis should be started as soon as the diagnosis is considered and continued for 24 to 36 hours. An exchange of transfusion shold be undertaken before and after the dialysis, together with an osmotic diuresis if appropriate. Continuous enteral feeding should be given, the quantity being adjusted to the baby's requirements.

Amino Acid Metabolism, Inborn Errors↗