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PubMed1999

Biodegradation of cyclohexylamine by Brevibacterium oxydans IH-35A.

A bacterial strain capable of growing on cyclohexylamine (CHAM) was isolated by using enrichment and isolation techniques. The strain isolated, strain IH-35A, was classified as a member of the genus Brevibacterium. The results of growth and enzyme studies are consistent with degradation of CHAM via cyclohexanone (CHnone), 6-hexanolactone, 6-hydroxyhexanoate, and adipate. Cell extracts obtained from this strain grown on CHAM contained CHAM oxidase, and the model for CHAM oxidation by this enzyme was similar to the model for deamino oxidation of amine by amine oxidase.

Biodegradation, Environmental↗
PubMed2002

Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase.

Cyclopentanone 1,2-monooxygenase, a flavoprotein produced by Pseudomonas sp. strain NCIMB 9872 upon induction by cyclopentanol or cyclopentanone (M. Griffin and P. W. Trudgill, Biochem. J. 129:595-603, 1972), has been utilized as a biocatalyst in Baeyer-Villiger oxidations. To further explore this biocatalytic potential and to discover new genes, we have cloned and sequenced a 16-kb chromosomal locus of strain 9872 that is herein reclassified as belonging to the genus COMAMONAS: Sequence analysis revealed a cluster of genes and six potential open reading frames designated and grouped in at least four possible transcriptional units as (orf11-orf10-orf9)-(cpnE-cpnD-orf6-cpnC)-(cpnR-cpnB-cpnA)-(orf3-orf4 [partial 3' end]). The cpnABCDE genes encode enzymes for the five-step conversion of cyclopentanol to glutaric acid catalyzed by cyclopentanol dehydrogenase, cyclopentanone 1,2-monooxygenase, a ring-opening 5-valerolactone hydrolase, 5-hydroxyvalerate dehydrogenase, and 5-oxovalerate dehydrogenase, respectively. Inactivation of cpnB by using a lacZ-Km(r) cassette resulted in a strain that was not capable of growth on cyclopentanol or cyclopentanone as a sole carbon and energy source. The presence of sigma(54)-dependent regulatory elements in front of the divergently transcribed cpnB and cpnC genes supports the notion that cpnR is a regulatory gene of the NtrC type. Knowledge of the nucleotide sequence of the cpn genes was used to construct isopropyl-beta-thio-D-galactoside-inducible clones of Escherichia coli cells that overproduce the five enzymes of the cpn pathway. The substrate specificities of CpnA and CpnB were studied in particular to evaluate the potential of these enzymes and establish the latter recombinant strain as a bioreagent for Baeyer-Villiger oxidations. Although frequently nonenantioselective, cyclopentanone 1,2-monooxygenase was found to exhibit a broader substrate range than the related cyclohexanone 1,2-monooxygenase from Acinetobacter sp. strain NCIMB 9871. However, in a few cases opposite enantioselectivity was observed between the two biocatalysts.

Catalysis↗
PubMed2000

Genetic analysis of a gene cluster for cyclohexanol oxidation in Acinetobacter sp. Strain SE19 by in vitro transposition.

Biological oxidation of cyclic alcohols normally results in formation of the corresponding dicarboxylic acids, which are further metabolized and enter the central carbon metabolism in the cell. We isolated an Acinetobacter sp. from an industrial wastewater bioreactor that utilized cyclohexanol as a sole carbon source. A cosmid library was constructed from Acinetobacter sp. strain SE19, and oxidation of cyclohexanol to adipic acid was demonstrated in recombinant Escherichia coli carrying a SE19 DNA segment. A region that was essential for cyclohexanol oxidation was localized to a 14-kb fragment on the cosmid DNA. Several putative open reading frames (ORFs) that were expected to encode enzymes catalyzing the conversion of cyclohexanol to adipic acid were identified. Whereas one ORF showed high homology to cyclohexanone monooxygenase from Acinetobacter sp. strain NCIB 9871, most of the ORFs showed only moderate homology to proteins in GenBank. In order to assign functions of the various ORFs, in vitro transposon mutagenesis was performed using the cosmid DNA as a target. A set of transposon mutants with a single insertion in each of the ORFs was screened for cyclohexanol oxidation in E. coli. Several of the transposon mutants accumulated a variety of cyclohexanol oxidation intermediates. The in vitro transposon mutagenesis technique was shown to be a powerful tool for rapidly assigning gene functions to all ORFs in the pathway.

Acinetobacter↗
PubMed2000

Conversion of 4-hydroxyacetophenone into 4-phenyl acetate by a flavin adenine dinucleotide-containing Baeyer-Villiger-type monooxygenase.

An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monomer with an M(r) of about 70,000 and contained one molecule of flavin adenine dinucleotide (FAD). The enzyme was specific for NADPH as the electron donor, and spectral studies showed rapid reduction of the FAD by NADPH but not by NADH. Other arylketones were substrates, including acetophenone and 4-hydroxypropiophenone, which were converted into phenyl acetate and 4-hydroxyphenyl propionate, respectively. The enzyme displayed Michaelis-Menten kinetics with apparent K(m) values of 47 microM for 4-hydroxyacetophenone, 384 microM for acetophenone, and 23 microM for 4-hydroxypropiophenone. The apparent K(m) value for NADPH with 4-hydroxyacetophenone as substrate was 17.5 microM. The N-terminal sequence did not show any similarity to other proteins, but an internal sequence was very similar to part of the proposed NADPH binding site in the Baeyer-Villiger monooxygenase cyclohexanone monooxygenase from an Acinetobacter sp.

Acetophenones↗
PubMed1999

Raised concentrations of aldehyde lipid peroxidation products in premature infants with chronic lung disease.

AIM: To indicate the extent of lipid peroxidation induced by oxidative stress, by measuring aldehyde end products in biological samples. METHODS: A highly specific gas chromatography and mass spectrometry (GC/MS) method was used to measure plasma concentrations of aliphatic aldehydes within the first week of life in 13 premature infants who subsequently developed chronic lung disease (CLD) and 11 infants without CLD (non-CLD). The oxime-tert-butyldimethylsilyl derivatives of aldehydes were analysed using 2,2,6,6-d4-cyclohexanone as the internal standard. RESULTS: All of the aldehydes measured were raised in those infants with CLD compared with non-CLD infants. Plasma concentrations of heptanal, 2-nonenal, and 4-hydroxynonenal (HNE) were significantly increased in CLD infants on the day of birth, while the differences in all aldehydes between the two groups were not significant at 4-6 days of age. Logistic regression analysis showed that the increase in these three aldehydes within the first 24 hours of life independently showed significant associations with the development of CLD. In particular, an HNE concentration of > or = 200 nM on day 0 was the best predictor for the early detection of CLD (odds ratio = 32.0), followed by a 2-nonenal concentration of > or = 150 nM (odds ratio = 16.0). CONCLUSIONS: These findings suggest that lipid peroxidation may have a role in the pathogenesis of neonatal CLD.

Aldehydes↗
PubMed1982

A cyclohexanecarboxylic acid utilizing yeast: isolation, identification, and nutritional characteristics.

A yeast capable of utilizing cyclohexanecarboxylic acid as sole carbon and energy source, strain KUY-6A, was isolated from soil by enrichment cultures. Taxonomical studies indicated that strain KUY-6A was Trichosporon cutaneum. Strain KUY-6A grew on a number of carboxylic acids. Among the cyclic compounds tested, cyclohexanecarboxylic acid was the best substrate. Cyclopentanecarboxylic acid, cycloheptanecarboxylic acid, cyclopentanone, cyclohexanone, and cyclopentanol also supported growth. In addition, the organism used the monocarboxylic acids, butyric, valeric, and caproic; the dicarboxylic acids succinic, glutaric, adipic, pimelic, and suberic; and the aromatic acids, benzoic and o-, m-, and p-hydroxybenzoic. The yeast did not require any vitamins for growth, although thiamine gave slight stimulation. The cell dry weight yield was 0.75 g from 1 g cyclohexanecarboxylic acid used.

Cyclohexanecarboxylic Acids↗
PubMed1996

Characterization of partial anaerobic metabolic pathway for 2,4,6-trinitrotoluene degradation by a sulfate-reducing bacterial consortium.

The anaerobic degradative pathway for metabolism of 2,4,6-trinitrotoluene (TNT) by a consortium of Desulfovibrio spp. isolated from a creek sediment was studied. This consortium has the metabolic capability to degrade TNT to fatty acids. The growth of the consortium and the metabolism of TNT were greatly enhanced in the presence of an additional carbon source like pyruvate. The optimal concentration of pyruvate for the maximum rate of TNT degradation was 15-20 mM. Various intermediates of TNT metabolism were identified. The first step in the pathway was reduction of TNT to 4-amino-2,6-dinitrotoluene and 2-amino-4,6-dinitrotoluene, which were further reduced to 2,4-diamino,6-nitrotoluene. The next intermediate to appear in the culture medium was nitrobenzoic acid, followed by cyclohexanone, 2-methyl pentanoic acid, butyric acid, and acetic acid. A study using radiolabeled TNT showed that no CO2 was produced from TNT during metabolism. The mass balance of the radiolabeled study showed that 49.6% of the TNT was converted to acetic acid, 28% was assimilated into biomass as trichloroacetic acid precipitable materials, and the rest was distributed as various TNT intermediates. Most Desulfovibrio spp. are incomplete oxidizers that are unable to carry out the terminal oxidation of organic substrates. The major end product of TNT metabolism was acetic acid. The bacteria grew on all the TNT intermediates tested as sole source of carbon, except on acetic acid, confirming that the Desulfovibrio spp. have the enzymes necessary for complete degradation of TNT to acetate.

Acetic Acid↗
PubMed1992

Signal transduction by the erythropoietin receptor: evidence for the activation of phospholipases A2 and C.

Erythropoietin (Ep) is the peptide growth factor whose actions on the erythroid progenitor cell induce terminal differentiation. However, the intracellular signaling system that is activated by Ep is poorly understood. Our previous studies have implicated the lipoxygenase metabolites of arachidonic acid in the actions of Ep. In this study, we report an early (30 s to 5 min) increase in levels of two lipoxygenase metabolites: leukotriene B4 (LTB4; 3- to 5-fold) and 12-hydroxyeicosatetraenoic acid (12-HETE; 2-fold). These responses were blocked by an antibody to Ep, by lipoxygenase inhibitors, or by 1,6-di[O-(carbamoyl)cyclohexanone oxime]hexane (RHC80267), an inhibitor of diacylglycerol (DAG) lipase. RHC 80267 also significantly inhibited Ep-mediated proliferation. Ep induced the release of [3H]arachidonic acid from cellular phospholipids at 5 min and also increased DAG accumulation at 1 min with a maximum increase of 68.2% over control seen at 30 min. No increase in levels of inositol trisphosphate or phosphatidic acid was observed in response to Ep. Taken together, these data suggest that the signal transduction pathway of the Ep receptor includes the activation of phospholipases A2 and C, resulting in the liberation of DAG and arachidonate and the subsequent formation of LTB4 and 12-HETE.

12-Hydroxy-5,8,10,14-eicosatetraenoic Acid↗
PubMed1980

Thermoregulation in Telazol (CI-744)-anesthetized rhesus monkey (Macaca mulatta).

Seven Telazol (CI-744)-[Telazol is an experimental drug (Parke, Davis) composed of two ingredients in equal amounts by weight: tiletamine HCl, designated chemically as 2-(ethylamino)-2-(2-thienyl)cyclohexanone-HCl, and zolazepam HCl, designated as 4-(o-fluorophenyl)-6,8-dihydro-1,3,8-trimethylpyrazolo-3,4-e 1,4 diazepin-7(IH)-one monohydrochloride] anesthetized rhesus monkeys (Macaca mulatta) were exposed to ambient temperatures (Ta) of 15, 23, 29, 35, and 38 degrees C to evaluate the effect of this dissociative anesthetic agent on thermoregulation. Thermal equilibrium in both anesthetized and control animals at Ta 15 degrees C was through peripheral vasoconstriction and metabolic heat production (M); shivering increased M in the anesthetized group to 1.7 times the resting M of 41.4 W x m-2. Both groups at Ta 38 degrees C regulated body temperature by vasodilation and increased skin evaporative heat loss (Esk) due to sweating. Anesthetized animals increased Esk from 6.4 W x m-2 at Ta 29 degrees C to 32.5 W x m-2 at Ta 38 degrees C. Panting was not observed in either group. Effective tissue thermal conductance was lowest at Ta 15 and 23 degrees C (6.9 and 7.6 W x m2 x degrees C-1, respectively), and increased with Ta's above 23 degrees C (45.0 W x m-2 at Ta 38 degrees C). These results indicate that Telazol-anesthetized monkeys maintain thermal balance at ambient temperatures from 15 to 38 degrees C, and that Telazol induces little or no impairment of thermoregulation in rhesus monkeys.

Anesthesia↗
PubMed1975

A safe and fast-acting surgical anesthetic for use in the guinea pig.

Ketamine [dl-2-(o-chlorophenyl)-2-(methylamino)cyclohexanone] hydrochloride was used in conjunction with Acepromazine [10-3-(dimethylamino)-propyl]phenothiazin-2-yl-methyl ketone] Maleate to produce surgical depth anesthesia in guinea pigs. In tests with 97 animals, an intramuscular injection of 44 mg/kg ketamine hydrochloride plus 2 mg Acepromazine Maleate was found to be effective in producing a surgical level of anesthesia within 2 min after administration. The anesthetic state lasted for an average of 1.5 h and could be safely extended by supplemental administrations of the drugs. This anesthetic combination was found to be fast acting, safe, and easily controlled.

Acepromazine↗
PubMed1994

Purification and characterization of 5 alpha-dihydrotestosterone 3 beta-hydroxysteroid dehydrogenase from mature pig testicular cytosol.

NADPH-dependent 5 alpha-dihydrotestosterone 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) was purified to apparent homogeneity from mature pig testicular cytosol. The purified enzyme catalyzed the conversion of 5 alpha-dihydrotestosterone (5 alpha-DHT) to 5 alpha-androstane-3 beta, 17 beta-diol. The molecular weight was estimated to be 31 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 28 kDa by gel filtration chromatography, indicating that the native 3 beta-HSD is a monomer. The isoelectric point of the purified enzyme was 5.8 as determined by chromatofocusing. The purified enzyme reduced not only 5 alpha-DHT but also 5 beta-DHT, 5 alpha(or 5 beta)-androstanedione, 5 alpha(or 5 beta)-dihydroprogesterone, prostaglandin E1, 13,14-dihydro-15-keto-prostaglandin F2 alpha, glyceladehyde, xylose and glucuronic acid. Moreover, the enzyme reduced other carbonyl compounds including aromatic aldehydes, aromatic ketones and quinones such as 4-nitrobenzaldehyde, 4-benzoylpyridine, phenylglyoxal, cyclohexanone and 9,10-phenanthrenequinone at high rates when compared with steroids, prostaglandins and sugars. The purified enzyme was inhibited by AgNO3, SH-reagent, disulfiram, hexesterol, stilbestrol, disulfiram and divalent cations such as Cu2+, Hg2+, Cd2+ and Co2+. Furthermore, the enzymatic properties of the purified enzyme, including catalytic activity, inhibitory effects by various agents and immunological properties, were compared with those of 3 alpha/beta-HSD enzymes from pig testicular cytosol.

3-Hydroxysteroid Dehydrogenases↗
PubMed1994

Structural components of beta-eudesmol essential for its potentiating effect on succinylcholine-induced neuromuscular blockade in mice.

beta-Eudesmol, a sesquiterpenoid alcohol isolated from Atractylodes lancea rhizoma, potentiates the neuromuscular blocking effect of succinylcholine (SuCh). The potentiating effect is greater in diabetic muscles than in normal ones. To identify the structural components of beta-eudesmol contributing to this action, we examined the potentiating effect of newly synthesized tertiary alcohols related to beta-eudesmol in phrenic nerve-diaphragm muscle preparations of normal and alloxan-diabetic mice. Potentiating effects were exhibited by cyclohexylidene derivatives but not by cyclohexanone or cyclohexanol derivatives. The compound 2-(3-hydroxy-3-methylbutyl)cyclohexylidene exhibited a potentiating effect, but 3-(3-hydroxy-3-methylbutyl)cyclohexylidene did not. These results indicate that both the presence of an exo-methylene attached to a cyclohexane ring and the distance between the exo-methylene and the hydroxy group in beta-eudesmol are involved in the potentiating effect on SuCh-induced neuromuscular blockade.

Animals↗
PubMed1997

Carbonyl reductase activity exhibited by pig testicular 20 beta-hydroxysteroid dehydrogenase.

The carbonyl reductase activity exhibited by pig testicular 20 beta-hydroxysteroid dehydrogenase (20 beta-HSD) was examined using a recombinant enzyme. Kinetic parameters were obtained for 48 carbonyl group-containing substrates, including aromatic aldehydes, aromatic ketones, cycloketones, quinones, aliphatic aldehydes and aliphatic ketones. 20 beta-HSD showed a high affinity towards quinones, such as 9,10-phenanthrenequinone, alpha-naphthoquinone and menadione (Km values of 4, 2 and 5 microM, respectively), and the substrate utilization efficiency (Vmax/Km) of the enzyme against these quinones was very high. Cyclohexanone and 2-methylcyclohexanone were also reduced with a high Vmax/Km value, but not cyclopentanone or 2-methylcyclopentanone. Various aromatic aldehydes and ketones including benzaldehyde- and acetophenone-derivatives were reduced by 20 beta-HSD. Especially, 4-nitrobenzaldehyde and 4-nitroacetophenone were reduced with high Vmax/Km values in the related compounds. The enzyme also reduced the pyridine-derivatives, 2-, 3-, and 4-benzoylpyridine, with the Vmax/Km value for 2-benzoylpyridine being the highest. 20 beta-HSD reduced aliphatic aldehydes and aliphatic ketones, but was more effective on the former. The correlation between the structure of carbonyl compounds and their substrate Vmax/Km is discussed.

20-Hydroxysteroid Dehydrogenases↗
PubMed2003

Trichloroacetylation of some cyclic enamines.

The pyrrolidine and morpholine enamines of cyclic ketones such as cyclohexanone and cyclopentanone were successfully diacetylated at alpha- and alpha'-positions with trichloroacetyl chloride using zinc catalyst. Morpholine enamines of the cyclic ketones gave acetylated morpholine in good yields besides the corresponding diacetylated cyclic enamines. When the same reactions were performed by using triethylamine without using zinc, monoacetylation products of the same enamines were synthesized.

Amines↗
PubMed2004

[Asymmetric reactions based on activation and structure control of molecule--asymmetric reaction of lithiated nucleophiles].

The methodology we developed relies on an external chiral coordinating reagent that forms a deaggregated chelate complex with organolithium reagents. Under the positive control of a chiral dimethyl ether of stilbenediol 4, an asymmetric conjugate addition reaction of organolithium reagents with unsaturated imines and esters proceeded successfully to yield the corresponding addition products with reasonably high stereoselectivity. The sense of stereochemistry is predictable based on a coordination model. The methodology has been extended to a catalytic asymmetric 1,2-addition reaction of organolithium reagents with imines. An enantiotopic group differentiating the opening of cyclohexene oxide with organolithium was also mediated by a chiral ligand. The asymmetric Horner-Wadsworth-Emmons reaction of phosphonates and Peterson reaction of alpha-silylester with 4-substituted cyclohexanone were another successful extension of the methodology. A three-component reagent of lithium ester enolate, lithium amide, and chiral diether reacts with imines to afford beta-lactam with reasonably high enantioselectivity. Tridentate aminoether ligands were also shown to affect the catalytic asymmetric addition of lithium ester enoaltes to imines, giving beta-lactams with high enantioselectivity. Asymmetric conjugate addition of lithium amide to enoates was mediated by a chiral diether ligand to give the beta-aminoester with high yield and enatioselectivity. The methodology has been successfully applied to an asymmetric synthesis of biologically potent compounds. Dihydrexidine, a promising anti-Parkinsonism candidate, and salsolidine, a representative isoquinoline alkaloid, have been synthesized using asymmetric addition reactions of organolithium reagents as the key steps.

Antiparkinson Agents↗
PubMed1997

[Asymmetric synthesis using chiral bases].

Studies have been made to design chiral bidentate lithium amides and chiral tetradentate amines, and to explore the use of these chiral bases for enantioselective formation and reactions of lithium enolates. Chiral bidentate lithium amides having a chiral amide nitrogen made by virtue of chelation were successfully applied to the enantioselective deprotonation reaction of prochiral cyclic ketones, the kinetic resolution of racemic cyclohexanone derivatives by deprotonation, and the regioselective deprotonation of optically active 3-keto steroids. Structures of some of these chiral bidentate lithium amides in the solid state and in solution were elucidated by X-ray and NMR spectroscopic analyses. By the use of chiral tetradentate amines, enantioselective reactions of lithium enolates with electrophiles, such as alkylation, protonation, and Michael addition, proceeded successfully. Examples of catalytic enantioselective deprotonation, alkylation, and protonation by the present strategy are also presented and discussed.

Magnetic Resonance Spectroscopy↗
PubMed2005

Stability of immobilized soybean lipoxygenase in selected organic solvent media.

The immobilization and biocatalysis of commercially purified soybean lipoxygenase (LOX) type I-B (EC 1.13.11.12) were investigated in organic solvent media. The results showed that the highest immobilization efficiencies of LOX, 30.6 and 29.3%, were obtained with DEAE-cellulose and modified Eupergit C250L supports, respectively. The biocatalysis of free and immobilized (Eupergit C250L/EDA) LOXs was investigated in different mixtures of hexane and a selected cosolvent (95:5 [v/v]). The results showed a 1.5 and a 1.6 increase in the activity of free and immobilized LOXs, respectively, using a mixture of hexane and 1,4-dioxane compared with that in hexane alone; however, cosolvents, including 2-octanone, 2-heptanone, 2-butanone, and cyclohexanone, displayed an inhibitory effect on LOX activity. In the mixture of 1,4-dioxane and hexane, LOX activity was dependent on the cosolvent concentration, which was increased with 1,4-dioxane up to 5% (v/v). The threshold 1,4-dioxane concentration (C50) and the incubation period (T50) at which 50% of the maximal enzyme activity was obtained for the free and immobilized LOXs were 6.7 and 8.9% (v/v) and 9.1 and 17.0 min, respectively.

Catalysis↗
PubMed1994

Flavoenzymes inhibited by indomethacin.

The effect of indomethacin on the activity of five different flavoenzymes, three dehydrogenases and six hydrosases, was determined. Indomethacin at concentration 1.0 mM inhibited the activity, in decreasing order of sensitivity, of the following flavoenzymes: D-amino acid oxidase (pig kidney), flavin-containing monooxygenases (pig liver microsomal), cyclohexanone monooxygenase (Acinetobacter), NADPH-quinone reductase (pig liver), and glutathione reductase (yeast), but it had no effect on the activity of glucose oxidase (Aspergillus) or liver microsomal NADPH-cytochrome P-450 reductase. Indomethacin was competitive with D-alanine for the D-amino acid oxidase (Ki=30 microM) and with NADPH for all other flavoenzymes sensitive to this compound (Kis 170-500 microM). While indomethacin also inhibited two of the three NAD(P)+-dependent dehydrogenases tested, the Kis were relatively high (<1, 500 microM), and of the six different hydrolases tested only one, liver microsomal esterase, was inhibited by indomethacin (Ki=600 microM). Indomethacin also inhibited aminopyrine demethylation catalyzed by the liver microsomal P-450 monooxygenase (Ki=1,000 microM). Although the exact mechanism for the inhibition of functionally different flavoenzymes sensitive to indomethacin is not known, the inhibition is probably not due to the detergent properties of this drug.

Cytochrome P-450 Enzyme Inhibitors↗