| isolation and identification of the reaction product of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase. | the reaction product of enzymic dehydrogenation of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde (hcms) was isolated. the analytical data (elemental analyses, ir spectra, mass spectra, proton nmr spectra, and uv spectra) showed that the product was not alpha-hydroxy-gamma-carboxymuconic acid (hcma), the expected primary product of hcms dehydrogenation, but a lactone of hcma. the structure of the lactone was tentatively determined as alpha-pyrone-4,6-dicarboxylic acid. hcms was converte ... | 1979 | 528534 |
| chemical modification of pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by diethyl pyrocarbonate. | diethyl pyrocarbonate inactivates pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase: ec 4.1.3.17] by a simple bimolecular reaction. the inactivation is not reversed by hydroxylamine. the ph curve of inactivation indicates the involvement of a residue with a pk of 8.8. several lines of evidence show that the inactivation is due to the modification of epsilon-amino groups of lysyl residues. although histidyl residue is also modified, ... | 1991 | 1794988 |
| purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from pseudomonas ochraceae grown on phthalate. | 4-hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase: ec 4.1.3.17] has been purified to homogeneity (about 770-fold purification, yield 11.4%) from pseudomonas ochraceae grown on phthalate. the enzyme has a molecular weight of 160,000 (gel filtration on bio-gel a-1.5m), a subunit molecular weight of 26,000 (sds-page) and an isoelectric point of 5.0 (isoelectric focusing). the enzyme requires divalent metal ions such as mg2+, mn2+, co2+, zn2+, and cd2+ for ... | 1990 | 2229032 |
| activation of pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by inorganic phosphate. | pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase: ec 4.1.3.17], one of the metal ion-requiring aldolases, is markedly activated by pi. the activation is reversible and can be observed in every step of enzyme purification. the extent of activation is almost independent of the metal ion used, but varies with each substrate. the cleavage of l-4-carboxy-4-hydroxy-2-oxoadipate, a physiological substrate of the enzyme, is most strongly ... | 1990 | 2229033 |
| interaction of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase with reactive blue 2 and related dyes. | steady-state kinetic analyses suggest that pseudomonas ochraceae 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde: nadp+ oxidoreductase [ec 1.2.1.45]) functions through an ordered bibi mechanism. the enzyme binds one nadp+ molecule per subunit with a kd of 4.8 +/- 0.8 microm. the enzyme is adsorbed to a blue sepharose cl-6b column and can be eluted therefrom with reagents having high affinity for the enzyme such as nadp+, nad+, atp, an ... | 1988 | 3170510 |
| purification and properties of gamma-oxalomesaconate hydratase from pseudomonas ochraceae grown with phthalate. | pseudomonas ochraceae produced inducibly a hydro-lyase which catalyzes the reversible conversion of gamma-oxalomesaconate into (-)-gamma-oxalocitramalate. the enzyme has been purified to homogeneity from the bacteria grown with phthalate. the enzyme was a dimeric protein (pi=4.9) with a mr of 68,000 and showed a high specificity for gamma-oxalomesaconate (km=14 microm) and (-)-gamma-oxalocitramalate (km=6.4 microm). equilibrium constant for the hydration of gamma-oxalomesaconate at ph 8.0 and 24 ... | 1985 | 3985968 |
| purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. | a hydrolase which catalyzes specifically the interconversion between 2-pyrone-4,6-dicarboxylate and 4-oxalmesaconate was purified about 410-fold with a 16% yield from cell-free extracts of pseudomonas ochraceae grown with phthalate. upon disc gel electrophoresis, the enzyme preparation gave a single band which was coincident with the enzyme activity. the molecular weight of the enzyme was estimated to be 31,000 by gel filtration on sephadex g-75 and 33,000 by sodium dodecyl sulfate gel electroph ... | 1983 | 6841353 |
| enzymes responsible for degradation of 4-oxalmesaconic acid in pseudomonas ochraceae. | the enzyme responsible for the degradation of 4-oxalmesaconate was partially purified from pseudomonas ochraceae grown with phthalate. column chromatography on deae-cellulose caused separation into two distinct enzymes, i and ii. 4-oxalmesaconate was converted into pyruvate and oxalacetate in the presence of mgcl2 and enzymes i and ii. optimum ph of the reaction was observed at ph 8.2 in tris-hcl buffer. mgcl2 could be replaced by mncl2 or cocl2. both enzymes were stable to heat-treatment at 65 ... | 1983 | 6841354 |
| genetic and biochemical characterization of a 2-pyrone-4, 6-dicarboxylic acid hydrolase involved in the protocatechuate 4, 5-cleavage pathway of sphingomonas paucimobilis syk-6. | sphingomonas paucimobilis syk-6 is able to grow on a wide variety of dimeric lignin compounds with guaiacyl moieties, which are converted into protocatechuate by the actions of lignin degradation enzymes in this strain. protocatechuate is a key metabolite in the syk-6 degradation of lignin compounds with guaiacyl moieties, and it is thought that it degrades to pyruvate and oxaloacetate via the protocatechuate 4,5-cleavage pathway. in a 10.5-kb ecori fragment carrying the protocatechuate 4,5-diox ... | 1999 | 9864312 |
| emendation of pseudomonas straminea iizuka and komagata 1963. | the description of pseudomonas straminae lizuka and komagata 1963 was emended with data newly obtained. the spelling of the name of this taxon is also corrected as pseudomonas straminea. strains that were previously named 'pseudomonas ochracea' were identified as p. straminea. | 2000 | 10939658 |
| cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from pseudomonas ochraceae ngj1. | a dna fragment that carried the gene (proa) encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase was cloned from the chromosomal dna of pseudomonas ochraceae ngj1, and the coding region was assigned to the nucleotide sequence based on the n-terminal amino acid sequence of the enzyme purified from the organism. the proa gene was 684 bp long, corresponding to a protein of 227 amino acid residues with a calculated molecular mass of 24,067 da. the genes encoding a putative transporter and a 4-oxalome ... | 2001 | 11826967 |
| recharacterization of pseudomonas fulva iizuka and komagata 1963, and proposals of pseudomonas parafulva sp. nov. and pseudomonas cremoricolorata sp. nov. | seven pseudomonas fulva strains obtained from culture collections were taxonomically studied. the seven strains were separated into three clusters (clusters i to iii) on the basis of 16s rrna gene sequences, and located phylogenetically in the genus pseudomonas sensu stricto. further, the strains were classified into 4 groups (groups i to iv) on the basis of dna-dna similarity. as a result, cluster i was split into groups i and ii. group i included the type strain of p. fulva and two strains, an ... | 2001 | 12483612 |
| characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in sphingomonas paucimobilis syk-6. | the protocatechuate (pca) 4,5-cleavage pathway is the essential metabolic route for degradation of low-molecular-weight products derived from lignin by sphingomonas paucimobilis syk-6. in the 10.5-kb ecori fragment carrying the genes for pca 4,5-dioxygenase (ligab), 2-pyrone-4,6-dicarboxylate hydrolase (ligi), 4-oxalomesaconate hydratase (ligj), and a part of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (ligc), we found the ligk gene, which encodes 4-carboxy-4-hydroxy-2-oxoadipate (c ... | 2003 | 12486039 |
| cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of pseudomonas ochraceae ngj1. | the 2-pyrone-4,6-dicarboxylate lactonase gene (prol), the protocatechuate 4,5-dioxygenase alpha and beta subunits genes (prooa and proob), and the 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase gene (prod) were cloned from the chromosomal dna of pseudomonas ochraceae ngj1. these genes were in the order proloaobd on the dna, and a possible transcription terminator sequence followed. the prol and prod genes were over-expressed in escherichia coli, and their gene products were purified fo ... | 2004 | 15277747 |
| pseudomonas argentinensis sp. nov., a novel yellow pigment-producing bacterial species, isolated from rhizospheric soil in cordoba, argentina. | during a study in the argentinian region of chaco (cordoba), some strains were isolated from the rhizosphere of grasses growing in semi-desertic arid soils. two of these strains, one isolated from the rhizospheric soil of chloris ciliata (strain ch01(t)) and the other from pappophorum caespitosum (strain pa01), were gram-negative, strictly aerobic rods, which formed yellow round colonies on nutrient agar. they produced a water-insoluble yellow pigment, and a fluorescent pigment was also detected ... | 2005 | 15879241 |
| pseudomonas segetis sp. nov., isolated from soil. | a gram-negative, aerobic bacterium, designated strain fr1439t, was isolated from the soil of dokdo in the republic of korea. the cells of strain fr1439t were catalase- and oxidase-positive, motile and rod-shaped. phylogenetic analysis of the 16s rrna gene sequence revealed that it represents a distinct line of descent within the genus pseudomonas. the levels of dna-dna relatedness between strain fr1439t and type strains of phylogenetically related species, namely pseudomonas flavescens, pseudomo ... | 2006 | 17082397 |
| role of cysteine residues in 4-oxalomesaconate hydratase from pseudomonas ochraceae ngj1. | 4-oxalomesaconate hydratase from pseudomonas ochraceae ngj1 is unstable in the absence of reducing reagents such as dithiothreitol, and strongly inhibited by 5,5'-dithiobis(2-nitrobenzoic acid) (dtnb). to study the role of cysteine residues in enzyme catalysis, the eight individual cysteine residues of the enzyme were replaced with serine residues by site-directed mutagenesis. the catalytic properties and chemical modification of wild- and mutant type-enzymes by dtnb showed that (i) none of eigh ... | 2007 | 17284837 |