Publications
| Title | Abstract | Year(sorted ascending) Filter | PMID Filter |
|---|
| purification of steroid-induced enzymes from pseudomonas testosteroni. | 1964 | 14209323 | |
| physical and chemical characterization of hydroxysteroid dehydrogenases from pseudomonas testosteroni. | 1964 | 14209324 | |
| [enzyme induction with steroids in pseudomonas testosteroni]. | 1965 | 4379247 | |
| enzymatic oxidation of steroids by cell-free extracts of pseudomonas testosteroni: isolation of cleavage products of ring a. | 1965 | 5217462 | |
| inhibition by 2'-deoxyadenosine of enzyme induction in pseudomonas testosteroni. | 1965 | 5218718 | |
| preparation of crystalline delta-5-3-ketosteroid isomerase from pseudomonas testosteroni. | 1965 | 5849828 | |
| reversibility of steroid delta-isomerase. 3. the soluble enzyme of pseudomonas testosteroni. | 1966 | 4287910 | |
| [contribution to the study of the active site of 3 (or 17)-beta-hydroxysteroid: nad oxidoreductase of pseudomonas testosteroni]. | 1967 | 4293245 | |
| [inhibition, with alkaloids, of the steroid-dependent enzyme induction in pseudomonas testosteroni]. | 1967 | 4384350 | |
| inhibition of 3-beta-hydroxysteroid dehydrogenase from pseudomonas testosteroni by various estrogenic and progestinic steroids. | 1967 | 6023578 | |
| inhibition of the steroid-induced synthesis of delta-5-3-ketosteroid isomerase in pseudomonas testosteroni by a new purine deoxyribonucleoside analog: 6-chloro-8-aza-9-cyclopentylpurine. | 1967 | 6033637 | |
| [fatty acids of the cell wall and the membrane of pseudomonas testosteroni]. | 1967 | 6053273 | |
| studies with the 3-alpha-hydroxysteroid dehydrogenase from pseudomonas testosteroni-enzyme-substrate complementarity as the basis of selectivity and steric specificity. | 1967 | 5597320 | |
| the metabolism of aromatic acids by pseudomonas testosteroni and p. acidovorans. | 1967 | 5602468 | |
| inhibition of deoxyribonucleic acid-directed ribonucleic acid polymerase by extracts of steroid-induced and noninduced pseudomonas testosteroni. | 1967 | 12325385 | |
| the metabolism of protocatechuate by pseudomonas testosteroni. | 1. protocatechuate 4,5-oxygenase, purified 21-fold from extracts of pseudomonas testosteroni, was examined in the ultracentrifuge and assigned a mol.wt. of about 140000. 2. when diluted, the enzyme rapidly lost activity during catalysis. inactivation was partially prevented by l-cysteine. 3. with a saturating concentration of protocatechuate (1.36mm), k(m) for oxygen was 0.303mm. this value is greater than the concentration of oxygen in water saturated with air at 20 degrees . 4. cell extracts c ... | 1968 | 5683506 |
| further studies of steoidal inhibitors of delpha5, 3beta-hydroxysteroid dehydrogenase and delta5-delta4, 3-ketosteroid isomerase in pseudomonas testosteroni and in bovine adrenals. | 1968 | 5697036 | |
| [on the inhibition by excess substrate of beta-hydroxysteroid dehydrogenase from pseudomonas testosteroni]. | 1968 | 4301944 | |
| [relationship between the structure of a steroid and the inducing effect on 3 alpha-hydroxysteroid: nad oxidoreductase of pseudomonas testosteroni]. | 1969 | 5345977 | |
| bacterial metabolism of arylsulfonates. i. benzene sulfonate as growth substrate for pseudomonas testosteroni h-8. | pseudomonas testosteroni h-8 utilizes as sole carbon source benzene sulfonate (bs), p-toluene sulfonate (pts), and ethylbenzene sulfonate (ebs) but not higher homologs. growth on bs was rapid (generation time, 3 hr) and efficient (y = 57), and resulted in accumulation of sulfate. as the culture is acid-sensitive, the medium must be heavily buffered to permit extensive growth. the bs oxidase system is inducible. cells grown on bs, but not glutamate, oxidized bs, pts, or ebs without lag (qo(2) = 5 ... | 1971 | 5553286 |
| [inhibition of a dna-dependent rna biosynthesis by a macromolecular fraction of non-induced cells of pseudomonas testosteroni]. | 1971 | 4939704 | |
| the amino acid sequence of 5 -3-ketosteroid isomerase of pseudomonas testosteroni. | 1971 | 5135313 | |
| requirement of two protein fractions for o-demethylase activity in pseudomonas testosteroni. | 1971 | 11945566 | |
| conformation of native pseudomonas testosteroni delta(5)-->(4) 3-oxosteroid isomerase. | 1972 | 11946627 | |
| inhibition of the 3-ketosteroid 5 - 4 -isomerase of pseudomonas testosteroni by some bromo-3-ketosteroid derivatives. | 1972 | 5017704 | |
| [determination of the characteristics of an inductor necessary for its interaction with a repressor in pseudomonas testosteroni]. | 1972 | 4119671 | |
| differentiation between pseudomonas testosteroni and p. acidovorans by gas chromatography. | 1972 | 4561033 | |
| [studies on rna polymerase dna complex from pseudomonas testosteroni]. | 1972 | 4649824 | |
| the regulation of the -ketoadipate pathway in pseudomonas acidovorans and pseudomonas testosteroni. | 1972 | 4657135 | |
| micellar aggregation of 5 -3-keto steroids lacking a polar c-17 group and its relation to the activity and specificity of the 5 - 4 -3-ketosteroid isomerase of pseudomonas testosteroni. | 1973 | 4683484 | |
| molecular weight determination and structural studies of pseudomonas testosteroni delta 5 leads to 4-3-oxosteroid isomerase (ec 5.3.3.1). | 1973 | 4753764 | |
| [relation between enzyme induction and testosterone metabolism in pseudomonas testosteroni]. | 1973 | 4803170 | |
| absolute configuration of a metabolite in the m-fission pathway of protocatechuate. | an aldolase, which is induced in pseudomonas testosteroni during growth with p-hydroxybenzoate, preferentially attacks the r form of 4-hydroxy-4-methyl-2-oxoglutarate, a metabolite of protocatechuate catabolism. | 1973 | 4347922 |
| steroid-receptor in pseudomonas testosteroni released by osmotic shock. | 1973 | 4363616 | |
| induction of steroid-binding activity in pseudomonas testosteroni. | 1973 | 4363617 | |
| degradation of protocatechuate in pseudomonas testosteroni by a pathway involving oxidation of the product of meta-fission. | in addition to catalyzing the hydrolysis of 4-carboxy-2-hydroxymuconic semialdehyde, formed by meta-fission of protocatechuate, pseudomonas testosteroni also possesses a nicotinamide adenine dinucleotide(phosphate)-linked dehydrogenase for this compound and can degrade protocatechuate to pyruvate and oxaloacetate. | 1973 | 4143957 |
| the degradation of l-histidine, imidazolyl-l-lactate and imidazolylpropionate by pseudomonas testosteroni. | 1. imidazol-5-ylpropionate and imidazol-5-yl-lactate are degraded by pseudomonas testosteroni via inducible pathways. 2. growth on either compound as the sole source of carbon results in the induction of the enzymes for histidine catabolism. 3. the pathway of histidine degradation in this organism, a non-fluorescent pseudomonad, is shown to be the same as that operating in pseudomonas fluorescens and pseudomonas putida. it consists of the successive formation of urocanate, imidazol-4-on-5-ylprop ... | 1973 | 4146796 |
| the control of the enzymes degrading histidine and related imidazolyl derivates in pseudomonas testosteroni. | 1. the induction of the enzymes for the degradation of l-histidine, imidazolylpropionate and imidazolyl-l-lactate in pseudomonas testosteroni was investigated. 2. the activities of histidine ammonia-lyase, histidine-2-oxoglutarate aminotransferase and urocanase are consistent with these enzymes being subject to co-ordinate control under most growth conditions. however, a further regulatory mechanism may be superimposed for histidase alone under conditions where degradation of histidine must take ... | 1973 | 4146797 |
| 3-hydroxybenzoate 4-hydroxylase from pseudomonas testosteroni. | 1973 | 4148586 | |
| affinity chromatography of 3-oxosteroid delta4--delta5-isomerase of pseudomonas testosteroni. | 1974 | 4367971 | |
| periplasmic steroid-binding proteins and steroid transforming enzymes of pseudomonas testosteroni. | 1974 | 4376195 | |
| influence of an 18-hydroxyl group on the interaction of oestrogens and hydroxysteroid oxidoreductases. | 1. partially purified 17beta-hydroxy steroid-nad(+) oxidoreductases, prepared from pseudomonas testosteroni (ec 1.1.1.51), human term placenta (ec 1.1.1.62) and the cytoplasmic fraction of rat liver (ec 1.1.1.-) were tested for their ability to catalyse the oxidoreduction of 18-hydroxyoestradiol-17beta and 18-hydroxyoestrone. the products of incubation were identified by chromatographic procedures and by mass spectrometry. 2. the pseudomonas enzyme catalysed both the oxidation of 18-hydroxyoestr ... | 1974 | 4824210 |
| enzymatic determination of bile acids. the presence of a new enzyme, a 12alpha-hydroxysteroid: nad-oxidoreductase in extracts from pseudomonas testosteroni. | 1974 | 4422066 | |
| amino acid sequence of a peptide containing the active cysteine residue of histidine ammonia-lyase. | 1. oxidized (polymerized) histidine ammonia-lyase from pseudomonas testosteroni was activated with dithiothreitol and the reduced disulphide-linked cysteine residues of the native enzyme were carboxymethylated with iodo[(14)c]acetate. 2. the activity of the carboxymethylated enzyme was similar to that of the polymerized form and approx. 15% of that of the fully reduced form. 3. a tryptic digest of the [(14)c]carboxymethylated enzyme contained only one radioactive peptide. 4. the amino acid seque ... | 1974 | 4422650 |
| proceedings: synthesis of rna and dna in isolated chromosome of pseudomonas testosteroni. | 1974 | 4461578 | |
| on the 3 alpha-hydroxysteroid dehydrogenase from pseudomonas testosteroni. purification and properties. | 1974 | 4137094 | |
| effect of testosterone-estradiol-binding globulin in the enzymic oxidoreduction of 17-oxygenated c19 steroids. | the effect of both testosterone-estradiol-binding globulin (tebg) and albumin on enzymic oxidoreduction of four 17-oxygenated c19 steroids by bacterial 17beta-hydroxysteroid:nad oxidoreductase from pseudomonas testosteroni was investigated. the decreased yields of products under presence of tebg were found in both directions of reversible enzymic reaction. this finding was unexpected in the case of enzymic reduction in which the opposite effect could be assumed with respect of high affinity of t ... | 1975 | 50994 |
| bacterial metabolism of arylsulfonates: role of meta cleavage in benzene sulfonate oxidation by pseudomonas testosteroni. | pseudomonas testosteroni h-8 oxidizes certain lower alkylbenzene sulfonates at rates inversely related to the length of the alkyl group. appreciable q(o)2 values were observed for benzene sulfonate (bs), toluene sulfonate (ts), and ethylbenzene sulfonate (ebs), but not for propylbenzene sulfonate (ps) and higher homologues. catechol oxidation was catalyzed by a constitutive catechol-2,3-oxygenase (ec 1.99.2.a). yellow meta cleavage products accumulated when bs-grown cells were exposed to catecho ... | 1975 | 163618 |
| enzymatic transformation of morphine by hydroxysteroid dehydrogenase from pseudomonas testosteroni. | eznyme preparations from pseudomonas testosteroni containing alpha- and beta- hydroxysteroid dehydrogenases catalyzed the oxidation of morphine and codeine by nicotinamide adenine dinucleotide. morphine was converted in relatively low yield into 14-hydroxymorphinone probably via morphinone as an intermediate. codeine was converted to codeinone and 14-hydroxycodeinone. only the conversions at the 6-position were carred out by the hydroxysteroid dehydrogenase. hydroxylation at the 14-position did ... | 1975 | 172013 |
| 3alpha-hydroxysteroid dehydrogenase from pseudomonas testosteroni: kinetic properties with nad and its thionicotinamide analogue. | the kinetics of 3alpha-hydroxysteroid : nad oxidoreductase (ec 1.1.1.50) from pseudomonas testosteroni (atcc 11996) have been investigated. the kinetic analysis based on initial activity measurements and product inhibition studies, indicates that the addition of substrate to the enzyme and the release of products from it, follows an obligatory order (ordered bi bi mechanism). the ability of the enzyme to utilize the thionicotinamide analogue of nad (snad) as cofactor has been investigated using ... | 1975 | 234846 |
| allantoin racemase: a new enzyme from pseudomonas species. | 1. allantoin racemase is a novel enzyme which catalyzes the conversion of s(+)-and r(minus)-allantoin into the racemate. 2. the enzyme is present in pseudomonas testosteroni, pseudomonas putida and five biotypes of pseudomonas fluorescens, but absent in a number of other pseudomonas species. 3. the enzyme of ps. testosteroni was purified 133-fold and exposes optimal activity at ph 8.0-8.2 and 50 degrees c. the enzyme is stable on heating for 15 min at 70 degrees c. 4. the enzyme appeared to be s ... | 1975 | 237557 |
| effect of protein concentration on the molecular weight of delta5-3-ketosteroid isomerase. | the molecular weight of delta-5-3-ketosteroid isomerase from pseudomonas testosteroni was determined by means of sedimentation equilibrium and exclusion chromatography over a wide range of enzyme concentrations in 0.2 m potassium phosphate buffer, ph 7.0. in addition, the sedimentation constant of the enzyme was determinded over an extended range of concentrations. the enzyme was found to have a molecular weight of 26,000 plus or equal to 1,000, suggesting that it is a dimer of identical or simi ... | 1975 | 237889 |
| purification and properties of malate dehydrogenase from pseudomonas testosteroni. | nicotinamide adenine dinucleotide-linked malate dehydrogenase has been purified from pseudomonas testosteroni (atcc 11996). the purification represents over 450-fold increase in specific activity. the amino acid composition of the enzyme was determined and found to be quite different from the composition of the malate dehydrogenases from animal sources as well as from escherichia coli. despite this difference, however, the data show that the enzymatic properties of the purified enzyme are remark ... | 1975 | 238957 |
| the purification and properties of l-histidine--2-oxoglutarate aminotransferase from pseudomonas testosteroni. | 1. inducible l-histidine--2-oxoglutarate aminotransferase was purified some 170-fold from extracts of pseudomonas testosteroni. 2. the preparation showed only one major component after electrophoresis on polyacrylamide gels, though additional minor bands were observed when samples concentrated on a deae-cellulose column were used. 3. the molecular weight of the enzyme was found to be approx. 70000 by chromatography on sephadex g-200. 4. the purification scheme produced enzyme that was inactive i ... | 1975 | 241324 |
| concentration-dependent association of delta5-3-ketosteroid isomerase of pseudomonas testosteroni. | gel chromatography and ultracentrifugation studies show that delta5-3-ketosteroid isomerase of pseudomonas testosteroni a dimer with a molecular weight of 26,800 at concentrations below 1 mg per ml, undergoes reversible, concentration-dependent association at higher enzyme concentrations. in the concentration range between 0.04 and 15.6 mg per ml, apparent molecular radii of 23 a to 36 a and molecular weights of 26,000 to 69,000 were observed. the latter value represents the weight average molec ... | 1975 | 1141206 |
| specificity of oxidation of bile-salt hydroxyl groups by crude extracts of pseudomonas testosteroni (atcc 11996) used in determining bile salts. | recent experimental evidence suggests that, presumably as a recent of mutation, crude extracts of pseudomonas testosteroni (atcc 11996) no contain amounts of 7alpha- and 12alpha-hydroxysteroid dehydrogenate activity that invalidate the results of bile-salt determinations. to confirm or deny this, we studied the specificity of hydroxysteroid dehydrogenase contained in crude extracts of currently available samples of this bacterium in the oxidation of bile-salt hydroxyl groups. the dehydrogenases ... | 1975 | 1164792 |
| chemical modification of amino acid residues associated with the delta-4-3-ketosteroid-dependent photoinactivation of delta-5-3-ketosteroid isomerase. | we have studied the accumulation of dibenzyldimethyl-ammonium ion (dda+) by respiring membrane vesicles of escherichia coli, as an index of the generation of an electrical gradient during respiration. nonrespiring vesicles accumulated dda+ when k+ efflux was induced by valinomycin or monactin. by various criteria this was shown to be the exchange of one cation for another, independent of metabolism and coupled entirely by electrical forces. uptake of dda+ by respiring vesicles was inhibited by i ... | 1975 | 1167545 |
| letter: pseudomonas testosteroni septicemia. | 1975 | 1180436 | |
| on the 3alpha-hydroxysteroid dehydrogenase from pseudomonas testosteroni. the effect of denaturing agents. | highly purified preparations of the 3alpha-hydroxysteroid:nad- oxidoreductase (e.c.1.1.1.50) from pseudomonas testosteroni (atcc 11996) which consist of two major isoenzymes, with traces of a third, have been split into two enzymatically inactive polypeptides a and b by the use of sodium dodecylsulphate, urea and guanidinium hydrochloride. both polypeptides have a molecular weight of 25,000 +/- 2,500 as shown by thin-layer gel chromatography and ultracentrifugations. they differ, however, in cha ... | 1975 | 1184284 |
| horse-liver alcohol dehydrogenase and pseudomonas testosteroni 3(17)beta-hydroxysteroid dehydrogenase transfer epimeric hydrogens from nadh to 17beta-hydroxy-5alpha-androstan-3-one. an exception to one of the alworth-bentley rules. | in the reduction of 17beta-hydroxy-5alpha-androstan-3-one to the 3beta-alcohol, horse liver alcohol dehydrogenase utilizes the 4-pro-r hydrogen of nadh whereas the 3(17)beta-hydroxysteroid dehydrogenase of pseudomonas testosteroni utulized the 4-pro-s hydrogen. these observations provide an exception to the rule proposed by alworth and bentley that with regard to the paired methylene hydrogens at c-4 of nadh and nadph "the stereospecificity of a particular reaction is fixed and does not vary wit ... | 1976 | 177288 |
| membrane bound 3beta and 17beta-hydroxysteroid dehydrogenase and its role in steroid transport in membrane vesicles of pseudomonas testosteroni. | 1976 | 180333 | |
| affinity chromatography of 3 alpha-hydroxysteroid dehydrogenase from pseudomonas testosteroni. use of n,n-dimethylformamide to prevent hydrophobic interactions between the enzyme and the ligand. | 1. the 3alpha-hydroxysteroid: nad+-oxidoreductase (ec 1.1.1.50) from pseudomonas testosteroni (atcc 11996) has been purified by affinity chromatography on sepharose 4b using glycocholic acid as ligand covalently bound through its carboxyl group to the ethylenediamine spacer. 2. the attachment of the enzyme to the substrate-containing matrix is greatly enhanced by the presence of nad+ suggesting that this enzyme has a compulsory ordered mechanism where nad+ binds to the enzyme before the steroid. ... | 1976 | 181083 |
| [chromosomal structures of pseudomonas testosteroni. i. isolation and characterization of the chromosomal complexes. (author's transl)]. | after lysis of pseydomonas testosteroni with lysozyme and non-ionic detergents different dna-protein complexes can be separated in 5-25% (w/v) neutral sucrose gradient. the protein to dna ratio of these complexes varies between 0.5-4.5 to 1, whereby the faster sedimenting forms contain more protein than the slower sedimenting ones. different initial rates of dnase digestion may indicate various degrees of dna packing in these complexes. the chromosomal complexes of pseudomonas testosteroni are r ... | 1976 | 132046 |
| [chromosomal structure of pseudomonas testosteroni. ii. activity of the endogenous rna-polymerase (author's transl)]. | after careful lysis the nucleoid of pseudomonas testosteroni can be isolated in three different forms with compact and unfolded dna structures. the released nucleoids contain endogenous dna-dependent rna-polymerase activity using the chromosomal dna as a template. rna synthesis is proportional to duration of rna-polymerase reaction and amount of dna-protein-complexes. the sensitivity towards ionic strength and rifampicin indicates that a part of rna-polymerase activity is tightly bound to the ch ... | 1976 | 136130 |
| effect of sulfhydryl and disulfide agents on 3beta and 17beta-hydroxysteroid dehydrogenase and on steroid uptake of pseudomonas testosteroni. | 1976 | 966766 | |
| temperature-sensitive rna synthesis during adaptive growth on testosterone of pseudomonas testosteroni. | 1976 | 979269 | |
| the involvement of the electron transport chain in uptake of testosterone by membrane vesicles of pseudomonas testosteroni. | 1976 | 1011843 | |
| phthalate metabolism in pseudomonas testosteroni: accumulation of 4,5-dihydroxyphthalate by a mutant strain. | a mutant strain of pseudomonas testosteroni blocked in phthalate catabolism converted phthalate into 4,5-dihydroxyphthalate. the latter compound was isolated, and its physical properties were determined. a stoichiometric conversion of the compound to protocatechuate was demonstrated spectrophotometrically with crude extracts of a protocatechuate 4,5-dioxygenase-deficient mutant. therefore, phthalate is metabolized through 4,5-dihydroxyphthalate and protocatechuate, which is further degraded by p ... | 1977 | 873893 |
| interaction of steroids with pseudomonas testosteroni 3-oxosteroid delta4--delta5-isomerase. | 1977 | 911812 | |
| a reinvestigation of the mechanism of pseudomonas testosteroni delta 5-3-ketosteroid isomerase. | the mechanism of the isomerisation of delta 5-3,17-androstenedione by the isomerase (3-oxosteroid delta 4-delta 5-isomerase, ec 5.3.3.1) of pseudomonas testosteroni has been reinvestigated with delta 5-[4-beta-2h]androstenedione as substrate in h2o and delta 5-androstenedione in 2h2o. a precise localisation of the label in delta 4-androstenendione has revealed that the previously reported 4 beta leads to 6 beta deuterium transfer accounts for only a part of the reaction. along with this process ... | 1977 | 922021 |
| [chromosomal structures of pseudomonas testosteroni. iv. effect of testosterone on rna-synthesis (author's transl)]. | testosterone degrading enzymes are synthesized de novo by bacterium p. testosteroni to utilize testosterone-like steroids as the only source of carbon. rna-synthesis of the whole lysate of testosterone-induced bacteria was found to be 15% reduced compared to the control, suggesting a cytoplasmatic factor which modulates chromatin associated rna-polymerase activity. | 1977 | 143827 |
| characterisation of an associate 17-beta-hydroxysteroid dehydrogenase activity and affinity labelling of the 3-alpha-hydroxysteroid dehydrogenase of pseudomonas testosteroni. | the 3-alpha-hydroxysteroid dehydrogenase and the 3-beta-hydroxysteroid dehydrogenase of pseudomonas testosteroni were purified to homogeneity by polyaerylamide gel electrophoresis using the following stages: deae cellulose chromatography, affinity chromatography on oestrone-aminocaproate sepharose and sephadex gel filtration. the pure 3-alpha-hydroxysteroid dehydrogenase was completely devoid of 3-beta-hydroxysteroid dehydrogenase activity but could oxidize estradiol 17-beta at an appreciable ra ... | 1977 | 607995 |
| 3(17)beta-hydroxysteroid dehydrogenase of pseudomonas testosteroni. a convenient purification and demonstration of multiple molecular forms. | 1977 | 193845 | |
| 3(17)beta-hydroxysteroid dehydrogenase of pseudomonas testosteroni. ligand binding properties. | the binding of nad and nadh to electrophoretically pure 3(17)beta-hydroxysteroid dehydrogenase of pseudomonas testosteroni was determined by fluorescence spectroscopy and gel filtration. four moles of cofactor are bound/mol of tetrameric enzyme; the binding sites are equivalent and independent. the dissociation constants for nad and nadh are 16 and 0.25 micronm, respectively. as measured by gel filtration in the absence of cofactor, 0.4 mol of estradiol-17 beta is bound/mol of tetrameric enzyme. ... | 1977 | 193846 |
| specific gonadotropin binding to pseudomonas maltophilia. | binding of 125i-labeled human chorionic gonadotropin to pseudomonas maltophilia is dependent on time, temperature, and ph and the binding to this procaryotic species is hormone-specific and saturable. the equilibrium dissociation constant is 2.3 x 10(-9) m. there are no cooperative interactions between binding sites (hill coefficient, 1.05). the number of sites is estimaated as 240 fmol/100 mug of protein. nacl and kcl, at concentrations from 1 to 10 mm, have no effect on binding. divalent catio ... | 1977 | 265583 |
| purine degradation in pseudomonas aeruginosa and pseudomonas testosteroni. | 1. adenine, hypoxanthine, xanthine and guanine are broken down in pseudomonas aeruginosa and pseudomonas testosteroni to allantoin by the concerted action of the enzymes adenine deaminase, guanine deaminase, nad+-dependent xanthine dehydrogenase and uricase. 2. uric acid is broken down by an unstable, membrane-bound uricase with an unusually low ph optimum. 3. in both strains adenine inhibits growth and xanthine dehydrogenase. a second type of inhibition is manifest only in ps. testosteroni and ... | 1977 | 407941 |
| hydroxysteroid dehydrogenases of pseudomonas testosteroni. separation of a 17 beta-hydroxysteroid dehydrogenase from the 3(17) beta-hydroxysteroid dehydrogenase and comparison of the two enzymes. | when a crude extract of pseudomonas testosteroni induced with testosterone was subjected to polyacrylamide gel electrophoresis, six bands that stained for 17 beta-hydroxysteroid dehydrogenase activity was observed. a protein fraction containing the enzyme corresponding to the fastest migrating band and devoid of the other hydroxysteroid dehydrogenase activities has been obtained. this preparation appears to be distinct from the previously isolated 3(17) beta-hydroxysteroid dehydrogenase (ec 1.1. ... | 1977 | 411517 |
| the purification and properties of urocanase from pseudomonas testosteroni. | urocanase (urocanate hydratase, ec 4.2.1.49) purified from pseudomonas testosteroni has a mol.wt. of 118000 determined by sedimentation-equilibrium analysis. ultracentrifugation in 6m-guanidine hydrochloride and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate show that the enzyme consists of two identical or very similar subunits. it is, like urocanase isolated from other sources, inhibited by reagents that react with carbonyl groups. although urocanase from ps. testosteroni is str ... | 1978 | 25660 |
| phthalate and 4-hydroxyphthalate metabolism in pseudomonas testosteroni: purification and properties of 4,5-dihydroxyphthalate decarboxylase. | phthalate is degraded through 4,5-dihydroxyphthalate and protocatechuate in pseudomonas testosteroni nh1000. the ezyme 4,5-dihydroxyphthalate decarboxylase, catalyzing the conversion of 4,5-dihydroxyphthalate to protocatechuate and carbon dioxide, was purified approximately 130-fold from phthalate-induced cells of a protocatechuate 4,5-dioxygenase-deficient mutant of p. testosteroni. the most purified preparation showed a single protein band on sodium dodecyl sulfate-acrylamide disc gel electrop ... | 1978 | 29563 |
| continuous dehydrogenation of a steroid with immobilized microbial cells: effect of an exogenous electron acceptor. | whole cells of pseudomonas testosteroni, induced to synthesize steroid-transforming enzymes beforehand, have been immobilized by entrapment in polyacrylamide gel. the immobilized cells have been used to catalyze the continuous delta1-dehydrogenation of reichstein's substance s under various conditions in the presence of phenazine methosulfate (pms), an electron acceptor for the cell-free delta1-dehydrogenase. the presence of pms substantially increases the rate of reaction when fed with the ster ... | 1978 | 623902 |
| formation of 5-[17beta-2h]androstene-3beta,17alpha-diol from 3beta-hydroxy-5-[17,21,21,21-2h]pregnen-20-one by the microsomal fraction of boar testis. | after incubation of 3beta-hydroxy-5-[17,21,21,21-2h]-pregnen-20-one with the microsomal fraction of boar testis, the metabolites were analyzed by gas chromatography and gas chromatography-mass spectrometry. the following metabolites were identified: 3beta,17alpha-dihydroxy-5-[21,21,21-3h]pregnen-20-one, 3beta-hydroxy-5-androsten-17-one, 5-androstene-3beta,17beta-diol, and 5-[17beta-2h]androstene-3beta,17alpha-diol. the presence of a 2h atom at the 17beta position of 5-androstene-3beta,17alpha-di ... | 1978 | 659416 |
| binding of steroids by a partially purified periplasmic protein from pseudomonas testosteroni. | 1979 | 41976 | |
| affinity partition of proteins in aqueous two-phase systems containing polyoxyethylene glycol-bound ligand and charged dextrans. | the partition of the delta 5 leads to 4 3-oxosteroid isomerase of pseudomonas testosteroni in aqueous two-phase systems containing both the macroligand, polyoxyethylene glycol-bound estradiol, and charged (cationic or anionic) dextrans has been studied. if the enzyme is well retained in the upper phase by an adequate amount of macroligand, it is possible to improve the removal of the contaminating proteins by extracting them into a lower phase containing positively or negatively charged dextran. ... | 1979 | 94912 |
| "affinity" chromatography of steroid-transforming enzymes with a non-steroidal ligand. | the chromatographic behaviour of an avian oestradiol-17 beta dehydrogenase, the 3(17) beta-hydroxy steroid dehydrogenase from pseudomonas testosteroni and cortisone reductase from streptomyces dehydrogenans was studied on columns of p-(phenoxypropoxy)aniline attached to cnbr-activated sepharose. the ligand was effective in adsorbing the oestradiol dehydrogenase from a partially purified extract of chicken liver, and the cortisone reductase was perferentially retained when mixtures of the three d ... | 1979 | 435242 |
| phosphate and soil binding: factors limiting bacterial degradation of ionic phosphorus-containing pesticide metabolites. | soils that had a high binding capacity for inorganic orthophosphate (pi) had reduced capacities to bind ionic alkyl phosphorus compounds. only ionic methylphosphonate (mpn) and ionic phenylphosphonate exhibited moderate binding. pseudomonas testosteroni used either mpn or pi as a sole phosphorus source and exhibited diauxic utilization of mpn and pi. the utilization of mpn was suppressed in the presence of pi. this suppression was abolished by a pi-binding soil. the soil did not have a significa ... | 1979 | 453832 |
| the effects of specific inhibitors and an antiserum of 3 beta and 17 beta-hydroxysteroid dehydrogenase of steroid uptake in pseudomonas testosteroni. | 1979 | 459502 | |
| localization of 3 beta and 17 beta-hydroxysteroid dehydrogenase in pseudomonas testosteroni. | 1979 | 459503 | |
| inhibition of the 3 beta-hydroxysteroid oxidoreductase of pseudomonas testosteroni by steroids. | 55 steroids of the estratriene and androstane type with substituents in pos. 16 alpha, 17 alpha or 17 beta were tested for inhibition of the 3beta-hydroxysteroid oxidoreductase of pseudomonas testosteroni. estratrien-3-ols were strong and competitive inhibitors (ki less than 1 micron). substituents in pos. 16 alpha of estradiol influenced the inhibitory activity distinctly. substituents in 17 alpha- or 17 beta-position were of slight influence. 3-methoxy estratrienes gave no inhibition of the en ... | 1979 | 467367 |
| the amino acid composition of histidine ammonialyase from pseudomonas putida ncib 10807. | the amino acid composition of histidine ammonia-lyase from pseudomonas putida ncib 10807 suggests that this enzyme may be different from the pseudomonas testosteroni ncib 10808 histidine ammonia-lyase, whose amino acid composition is known. | 1979 | 488259 |
| protection of substrate against enzymatic action by binding to proteins. dependence upon enzyme and binding protein. | in fetal or adult rats estradiol is carried in the plasma by alpha-fetoprotein or albumin. the protection of the carriers toward enzymatic oxidation by 17 beta-hydroxysteroid dehydrogenase from rat liver has been studied. concentrations of carrier protein and estradiol were adjusted to give free estradiol concentrations varying from km/10 to km/100 and the ratio of the catalytic velocity to that observed for the same concentration of free estradiol in the absence of carrier protein were recorded ... | 1980 | 6156164 |
| influence of the position of the double bond in steroid substrates on the efficiency of the proton-transfer reaction by pseudomonas testosteroni 3-oxo-steroid delta 4-delta 5-isomerase. | studies of the proton-transfer reaction by pseudomonas testosteroni 3-oxo steroid delta(4)-delta(5)-isomerase with delta(5(6))- and delta(5(10))-steroid substrates demonstrate the importance of the position of the double bond for the efficiency of the isomerization process. thus 3-oxo-delta(5(6))-substrates have markedly high k(cat.) values, whereas those of 3-oxo-delta(5(10))-substrates are very low and their apparent k(m) values approach equilibrium dissociation constants. the first step in th ... | 1980 | 6248031 |
| [isolation and study of a bacteriophage of pseudomonas testosteroni]. | a virulent phage specific for pseudomonas testosteroni is described. this phage have a regular icosahedral head (52 nm between opposite angles) and a contractile tail (165 x 8 nm) but no fibers on. the buoyant density is 1,51 +/- 0,01 g/ml. the nucleic acid is an desoxyribonucleic acid with a density of 1,696 +/- 0,03 g/ml and a gc% between 33,7 and 39,7. | 1980 | 6451268 |
| antibodies to pseudomonas testosteroni 3-oxosteroid delta 4-delta 5-isomerase. | 1980 | 6774719 | |
| membrane-bound dehydrogenases of pseudomonas testosteroni. | 1980 | 6931945 | |
| bioconversion of m-hydroxybenzoate to 2,3-dihydroxybenzoate by mutants of pseudomonas testosteroni. | mutans of pseudomonas testosteroni were isolated for their inability to grow on m-hydroxybenzoate as sole carbon source. these mutants hydroxylated m-hydroxybenzoate for form 2,3-dihydroxybenzoate in high yeilds. the bioconversion described in this report represents the first reported example of 3-hydroxybenzoate 2-hydroxylase activity. | 1980 | 7354000 |
| the purification and characterization of delta 5-3-ketosteroid isomerase from pseudomonas putida, a cysteine-containing isomerase. | a delta 5-3-ketosteroid isomerase (ec 5.3.3.1) has been isolated from pseudomonas putida biotype b and purified to homogeneity. this previously undescribed steroid isomerase resembles that isolated from pseudomonas testosteroni (talalay, p., and wang, v.s. (1955) biochim. biophys. acta 18, 300-301). the enzyme is induced by various steroids, has a subunit molecular weight of 13,750 +/- 250, a pi of 4.8 +/- 0.1 has a specific activity of 40,000 units/mg, using 5-androstene-3,17-dione as the subst ... | 1980 | 7358699 |
| on the number of steroid-binding sites of delta 5-3-oxosteroid isomerase. | the number of steroid-binding sites in delta 5-3-oxosteroid isomerase of pseudomonas testosteroni (ec 5.3.3.1) has been determined from measurements of the red shift of the ultraviolet chromophore of 19-nortestosterone upon binding to the enzyme. the experiments include spectroscopic measurements when limiting concentrations of either 19-nortestosterone or isomerase are titrated with varying concentrations of the complementary ligand. analysis of the results indicates one binding site per subuni ... | 1980 | 7371643 |
| irreversible inactivation of delta 5-3-ketosteroid isomerase of pseudomonas testosteroni by acetylenic suicide substrates. mechanism of formation and properties of the steroid-enzyme adduct. | 1981 | 7240247 | |
| a reinvestigation of the mechanism of delta 5-3-ketosteroid isomerase from bovine adrenal glands. | the mechanism of the isomerization of androst-5-ene 3,17-dione by the isomerase of bovine adrenals has been reinvestigated using the methodology previously developed for the study of the bacterial enzyme of pseudomonas testosteroni. however, owing to the lower activity of the mammalian enzyme, competitive non-enzymic reaction cannot be neglected. it has been shown that even in the absence of spontaneous isomerization, epimerization and exchange of the label on c4 takes place in the buffer. this ... | 1981 | 7284399 |
| inactivation of delta 5-3-oxo steroid isomerase with active-site-directed acetylenic steroids. | several steroid analogues containing conjugated acetylenic ketone groups as part of a seco-ring structure or as substituents on the intact steroid system are irreversible inhibitors of delta 5-3-oxo steroid isomerase (ec 5.3.3.1) from pseudomonas testosteroni. thus 10 beta-(1-oxoprop-2-ynyl)oestr-4-ene-3,17-dione (i), 5,10-seco-oestr-4-yne-3,10,17-trione (ii), 17 beta-hydroxy-5,10-seco-oestr-4-yne-3,10-dione (iii) and 17 beta-(1-oxoprop-2-ynyl)androst-4-en-3-one (iv) irreversibly inactivate isom ... | 1981 | 7305923 |