Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Hydroxybenzoates”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,081 records · Page 60Linked to original sources
PubMed2001

Cloning and genetic characterization of dca genes required for beta-oxidation of straight-chain dicarboxylic acids in Acinetobacter sp. strain ADP1.

A previous study of deletions in the protocatechuate (pca) region of the Acinetobacter sp. strain ADP1 chromosome revealed that genes required for utilization of the six-carbon dicarboxylic acid, adipic acid, are linked to the pca structural genes. To investigate the genes involved in adipate catabolism, a 33.8-kb SacI fragment, which corrects a deletion spanning this region, was cloned. In addition to containing known pca, qui, and pob genes (for protocatechuate, quinate, and 4-hydroxybenzoate dissimilation), clone pZR8000 contained 10 kb of DNA which was the subject of this investigation. A mutant strain of Escherichia coli DH5alpha, strain EDP1, was isolated that was able to utilize protocatechuate and 4-hydroxybenzoate as growth substrates when EDP1 cells contained pZR8000. Sequence analysis of the new region of DNA on pZR8000 revealed open reading frames predicted to be involved in beta-oxidation. Knockouts of three genes implicated in beta-oxidation steps were introduced into the chromosome of Acinetobacter sp. strain ADP1. Each of the mutants was unable to grow with adipate. Because the mutants were affected in their ability to utilize additional saturated, straight-chain dicarboxylic acids, the newly discovered 10 kb of DNA was termed the dca (dicarboxylic acid) region. Mutant strains included one with a deletion in dcaA (encoding an acyl coenzyme A [acyl-CoA] dehydrogenase homolog), one with a deletion in dcaE (encoding an enoyl-CoA hydratase homolog), and one with a deletion in dcaH (encoding a hydroxyacyl-CoA dehydrogenase homolog). Data on the dca region should help us probe the functional significance and interrelationships of clustered genetic elements in this section of the Acinetobacter chromosome.

Acinetobacter↗
PubMed2005

Metabolism of bismuth subsalicylate and intracellular accumulation of bismuth by Fusarium sp. strain BI.

Enrichment cultures were conducted using bismuth subsalicylate as the sole source of carbon and activated sludge as the inoculum. A pure culture was obtained and identified as a Fusarium sp. based on spore morphology and partial sequences of 18S rRNA, translation elongation factor 1-alpha, and beta-tubulin genes. The isolate, named Fusarium sp. strain BI, grew to equivalent densities when using salicylate or bismuth subsalicylate as carbon sources. Bismuth nitrate at concentrations of up to 200 muM did not limit growth of this organism on glucose. The concentration of soluble bismuth in suspensions of bismuth subsalicylate decreased during growth of Fusarium sp. strain BI. Transmission electron microscopy and energy-dispersive spectroscopy revealed that the accumulated bismuth was localized in phosphorus-rich granules distributed in the cytoplasm and vacuoles. Long-chain polyphosphates were extracted from fresh biomass grown on bismuth subsalicylate, and inductively coupled plasma optical emission spectrometry showed that these fractions also contained high concentrations of bismuth. Enzyme activity assays of crude extracts of Fusarium sp. strain BI showed that salicylate hydroxylase and catechol 1,2-dioxygenase were induced during growth on salicylate, indicating that this organism degrades salicylate by conversion of salicylate to catechol, followed by ortho cleavage of the aromatic ring. Catechol 2,3-dioxygenase activity was not detected. Fusarium sp. strain BI grew with several other aromatic acids as carbon sources: benzoate, 3-hydroxybenzoate, 4-hydroxybenzoate, gentisate, d-mandelate, l-phenylalanine, l-tyrosine, phenylacetate, 3-hydroxyphenylacetate, 4-hydroxyphenylacetate, and phenylpropionate.

Biomass↗
PubMed1967

Inhibition of microorganisms by topical anesthetics.

The effect of various topical anesthetics and their preservatives on the growth of Pseudomonas aeruginosa, Staphyloccoccus albus, and Candida albicans was investigated. The topical anesthetics were proparacaine HCl, tetracaine HCl, cocaine HCl, and benoxinate HCl. The preservatives were chlorobutanol and butyl p-hydroxybenzoate. Proparacaine inhibited C. albicans but not P. aeruginosa or S. albus. All three test organisms were inhibited to varying degrees by tetracaine, benoxinate, cocaine, chlorobutanol, and butyl p-hydroxybenzoate.

Journal Article↗
PubMed2006

4-Chlorobenzoate uptake in Comamonas sp. strain DJ-12 is mediated by a tripartite ATP-independent periplasmic transporter.

The fcb gene cluster involved in the hydrolytic dehalogenation of 4-chlorobenzoate is organized in the order fcbB-fcbA-fcbT1-fcbT2-fcbT3-fcbC in Comamonas sp. strain DJ-12. The genes are operonic and inducible with 4-chloro-, 4-iodo-, and 4-bromobenzoate. The fcbT1, fcbT2, and fcbT3 genes encode a transporter in the secondary TRAP (tripartite ATP-independent periplasmic) family. An fcbT1T2T3 knockout mutant shows a much slower growth rate on 4-chlorobenzoate compared to the wild type. 4-Chlorobenzoate is transported into the wild-type strain five times faster than into the fcbT1T2T3 knockout mutant. Transport of 4-chlorobenzoate shows significant inhibition by 4-bromo-, 4-iodo-, and 4-fluorobenzoate and mild inhibition by 3-chlorobenzoate, 2-chlorobenzoate, 4-hydroxybenzoate, 3-hydroxybenzoate, and benzoate. Uptake of 4-chlorobenzoate is significantly inhibited by ionophores which collapse the proton motive force.

Adenosine Triphosphate↗
PubMed1970

Involvement of the protocatechuate pathway in the metabolism of mandelic acid by Aspergillus niger.

Cell-free extracts of Aspergillus niger UBC 814 grown in the presence of dl-mandelate oxidized both d(-)- and l(+)-mandelate via benzoylformate and benzaldehyde to benzoate. dl-p-Hydroxymandelate was oxidized, presumably through a parallel pathway, to p-hydroxybenzoate. A particulate d(-)-mandelate dehydrogenase and a supernatant fraction l(+)-mandelate dehydrogenase converted their respective substrates to benzoylformate. Both flavine adenine dinucleotide and flavine mononucleotide showed a stimulatory effect on the activity of the l(+)-mandelate dehydrogenase. Benzoylformate was decarboxylated to benzaldehyde by an enzyme requiring thiamine pyrophosphate for maximal activity. Two benzaldehyde dehydrogenases dependent on nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), respectively, for their activity dehydrogenated benzaldehyde to benzoate. In the presence of reduced NADP (NADPH), benzoate was oxidized via p-hydroxybenzoate and protocatechuate. Reduced NAD could not replace NADPH. Sensitive methods of assay for d(-)-mandelate dehydrogenase and benzoylformate decarboxylase are described. The fungal pathway is compared with these systems in bacteria.

Aspergillus↗
PubMed1971

Dissimilation of aromatic compounds by Alcaligenes eutrophus.

The range of aromatic compounds that support the growth of Alcaligenes eutrophus has been determined, and the pathways used for the dissimilation of these substrates have been explored, largely by enzymatic analyses. The beta-ketoadipate pathway operates in the dissimilation of benzoate and p-hydroxybenzoate; the genetisate pathway, in the dissimilation of m-hydroxybenzoate; and the meta cleavage pathway, in the dissimilation of phenol and p-cresol. l-Tryptophan is oxidized via anthranilate; but the metabolic fate of anthranilate was not established. The metabolism of the three stereoisomers of muconic acid was also examined.

Adipates↗
PubMed1972

Inducible uptake system for -carboxy-cis, cis-muconate in a permeability mutant of Pseudomonas putida.

A procedure for the large-scale enzymatic synthesis of beta-carboxymuconate is described. When used as a growth substrate, beta-carboxymuconate selected for mutant strains of Pseudomonas putida that were permeable to polycarboxylic acid intermediates of the beta-ketoadipate pathway. One mutant organism, strain PRS2110, was investigated in detail. It differed from the parental strain in that it possessed a beta-carboxymuconate uptake system that was formed when the compound was supplied exogenously to the cells. The uptake system was not induced by beta-carboxymuconate supplied endogenously during growth with p-hydroxybenzoate. These observations suggested that beta-carboxymuconate was contained within a physical compartment of enzymes during growth with p-hydroxybenzoate. Support for this hypothesis came from the demonstration that enzymes of the beta-ketoadipate pathway were held together by weak chemical interactions during the chromatography of crude extracts of benzoategrown P. putida on diethylaminoethyl-cellulose columns.

Adipates↗
PubMed1975

Pathways for the degradation of m-cresol and p-cresol by Pseudomonas putida.

A comparison of the oxidation rates of various compounds by whole cells of Pseudomonas putida 3, 5 indicated that m-cresol is metabolized by oxidation to 3-hydroxybenzoate followed by hydroxylation to gentisate, the ring-fission substrate, when grown with 3, 5-xylenol. However, when m-cresol was the growth substrate, similar experiments suggested a different pathway involving a methyl-substituted catechol, and ring-fission by meta cleavage. Assays of ring-fission enzymes in cell-free extracts confirmed that different pathways are induced by the two growth substrates. 3, 5-Xylenol-grown cells contained high levels of gentisate oxygenase and only very small amounts of catechol oxygenase, whereas gentisate ocygenase could not be detected in m-cresol-grown cells, but levels of catechol oxygenase were greatly increased. Extracts of m-cresol-grown cells also contained 2-hydroxymuconic semialdehyde dehydrogenase and hydrolase, whose specificities enable them to metabolize the ring-fission products from catechol, 3-methylcatechol, and 4-methylcatechol. This catechol pathway is also used by m-cresol-grown cells for p-cresol metabolism. In contrast, the results for cells grown with p-cresol point to an alternative pathway involving oxidation to 4-hydroxybenzoate and hydrosylation to protocatechuate as ring-fission substrate. Extracts of these cells contained high levels of protocatechuate oxygenase and only small amounts of catechol oxygenase.

Adipates↗
PubMed1984

Aromatic acids are chemoattractants for Pseudomonas putida.

A quantitative capillary assay was used to show that aromatic acids, compounds that are chemorepellents for Escherichia coli and Salmonella sp., are chemoattractants for Pseudomonas putida PRS2000. The most effective attractants were benzoate; p-hydroxybenzoate; the methylbenzoates; m-, p-, and o-toluate; salicylate; DL-mandelate; beta-phenylpyruvate; and benzoylformate. The chemotactic responses to these compounds were inducible. Taxis to benzoate and m-toluate was induced by beta-ketoadipate, a metabolic intermediate formed when benzoate is dissimilated via enzymes specified by chromosomal genes. Benzoylformate taxis was induced by benzoylformate and L(+)-mandelate. Taxis to mandelate, benzoylformate, and beta-phenylpyruvate was exhibited by cells grown on mandelate, but not by cells grown on benzoate. Cells grown on benzoate were chemotactic to benzoate, the toluates, p-hydroxybenzoate, and salicylate. These results show that P. putida synthesizes at least two distinct chemoreceptors for aromatic acids. Although DL-mandelate was an effective attractant in capillary assays, additional experiments indicated that the cells were actually responding to benzoylformate, a metabolite formed from mandelate. With the exception of mandelate taxis, chemotaxis to aromatic acids was not dependent on the expression of pathways for aromatic degradation. Therefore, the tactic responses exhibited by cells cannot be attributed to an effect of the oxidation of aromatic acids on the energy metabolism of cells.

Amino Acids↗
PubMed1988

Anaerobic metabolism of phthalate and other aromatic compounds by a denitrifying bacterium.

The anaerobic metabolism of phthalate and other aromatic compounds by the denitrifying bacterium Pseudomonas sp. strain P136 was studied. Benzoate, cyclohex-1-ene-carboxylate, 2-hydroxycyclohexanecarboxylate, and pimelate were detected as predominant metabolic intermediates during the metabolism of three isomers of phthalate, m-hydroxybenzoate, p-hydroxybenzoate, and cyclohex-3-ene-carboxylate. Inducible acyl-coenzyme A synthetase activities for phthalates, benzoate, cyclohex-1-ene-carboxylate, and cyclohex-3-ene-carboxylate were detected in the cells grown on aromatic compounds. Simultaneous adaptation to these aromatic compounds also occurred. A similar phenomenon was observed in the aerobic metabolism of aromatic compounds by this strain. A new pathway for the anaerobic metabolism of phthalate and a series of other aromatic compounds by this strain was proposed. Some properties of the regulation of this pathway were also discussed.

Anaerobiosis↗
PubMed1988

Denitrification by a soil bacterium with phthalate and other aromatic compounds as substrates.

A soil bacterium, Pseudomonas sp. strain P136, was isolated by selective enrichment for anaerobic utilization of o-phthalate through nitrate respiration. o-Phthalate, m-phthalate, p-phthalate, benzoate, cyclohex-1-ene-carboxylate, and cyclohex-3-ene-carboxylate were utilized by this strain under both aerobic and anaerobic conditions. m-Hydroxybenzoate and p-hydroxybenzoate were utilized only under anaerobic conditions. Protocatechuate and catechol were neither utilized nor detected as metabolic intermediates during the metabolism of these aromatic compounds under both aerobic and anaerobic conditions. Cells grown anaerobically on one of these aromatic compounds also utilized all other aromatic compounds as substrates for denitrification without a lag period. On the other hand, cells grown on succinate utilized aromatic compounds after a lag period. Anaerobic growth on these substrates was dependent on the presence of nitrate and accompanied by the production of molecular nitrogen. The reduction of nitrite to nitrous oxide and the reduction of nitrous oxide to molecular nitrogen were also supported by anaerobic utilization of these aromatic compounds in this strain. Aerobically grown cells showed a lag period in denitrification with all substrates tested. Cells grown anaerobically on aromatic compounds also consumed oxygen. No lag period was observed for oxygen consumption during the transition period from anaerobic to aerobic conditions. Cells grown aerobically on one of these aromatic compounds were also adapted to utilize other aromatic compounds as substrates for respiration. However, cells grown on succinate showed a lag period during respiration with aromatic compounds. Some other characteristic properties on metabolism and regulation of this strain are also discussed for their physiological aspects.

Aerobiosis↗
PubMed1989

Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium.

Anoxic cell extracts of a denitrifying bacterial isolate (PC-07) were shown to oxidize p-cresol to p-hydroxybenzoate. Oxidation of the substrate was independent of molecular oxygen and required nitrate as the natural terminal electron acceptor. Two enzyme activities were implicated in the pathway utilized by PC-07. A p-cresol methylhydroxylase mediated the oxidation of p-cresol to p-hydroxybenzaldehyde, which was further oxidized to p-hydroxybenzoate by an NAD+-dependent dehydrogenase. The PC-07 methylhydroxylase was partially purified by anion-exchange chromatography. The protein appeared to be a multifunctional flavocytochrome, which first oxidized p-cresol to p-hydroxybenzyl alcohol, which was then oxidized to p-hydroxybenzaldehyde. The identity of the aldehyde was confirmed by mass spectroscopy. The PC-07 methylhydroxylase had a limited substrate range and required an alkyl-substituted phenolic ring with a hydroxyl group in the para position. From the available evidence, p-cresol, a naturally occurring phenol, exhibited the greatest affinity to the enzyme and therefore may be its natural substrate.

Anaerobiosis↗
PubMed1990

Expression of an aromatic-dependent decarboxylase which provides growth-essential CO2 equivalents for the acetogenic (Wood) pathway of Clostridium thermoaceticum.

The acetogen Clostridium thermoaceticum generates growth-essential CO2 equivalents from carboxylated aromatic compounds (e.g., 4-hydroxybenzoate), and these CO2 equivalents are likely integrated into the acetogenic pathway (T. Hsu, S. L. Daniel, M. F. Lux, and H. L. Drake, J. Bacteriol. 172:212-217, 1990). By using 4-hydroxybenzoate as a model substrate, an assay was developed to study the expression and activity of the decarboxylase involved in the activation of aromatic carboxyl groups. The aromatic-dependent decarboxylase was induced by carboxylated aromatic compounds in the early stages of growth and was not repressed by glucose or other acetogenic substrates; nonutilizable carboxylated aromatic compounds did not induce the decarboxylase. The decarboxylase activity displayed saturation kinetics at both whole-cell and cell extract levels, was sensitive to oxidation, and was not affected by exogenous energy sources. However, at the whole-cell level, metabolic inhibitors decreased the decarboxylase activity. Supplemental biotin or avidin did not significantly affect decarboxylation. The aromatic-dependent decarboxylase was specific for benzoates with a hydroxyl group in the para position of the aromatic ring; the meta position could be occupied by various substituent groups (-H, -OH, -OCH3, -Cl, or -F). The carboxyl carbon from [carboxyl-14C] vanillate went primarily to 14CO2 in short-term decarboxylase assays. During growth, the aromatic carboxyl group went primarily to CO2 under CO2-enriched conditions. However, under CO2-limited conditions, the aromatic carboxyl carbon went nearly totally to acetate, with equal distribution between the carboxyl and methyl carbons, thus demonstrating that acetate could be totally synthesized from aromatic carboxyl groups. In contrast, when cocultivated (i.e., supplemented) with CO under CO2-limited conditions, the aromatic carboxyl group went primarily to the methyl carbon of acetate.

Acetates↗
PubMed1995

Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate.

The first step of anaerobic benzoate degradation is the formation of benzoyl-coenzyme A by benzoate-coenzyme A ligase. This enzyme, purified from Rhodopseudomonas palustris, is maximally active with 5 microM benzoate. To study the molecular basis for this reaction, the benzoate-coenzyme A ligase gene (badA) was cloned and sequenced. The deduced amino acid sequence of badA showed substantial similarity to other coenzyme A ligases, with the highest degree of similarity being that to 4-hydroxybenzoate-coenzyme A ligase (50% amino acid identity) from R. palustris. A badA mutant that was constructed had barely detectable levels of ligase activity when cell extracts were assayed at 10 microM benzoate. Despite this, the mutant grew at wild-type rates on benzoate under laboratory culture conditions (3 mM benzoate), and mutant cell extracts had high levels of ligase activity when assayed at a high concentration of benzoate (1 mM). This suggested that R. palustris expresses, in addition to BadA, a benzoate-activating enzyme(s) with a relatively low affinity for benzoate. A possible role of 4-hydroxybenzoate-coenzyme A ligase (encoded by hbaA) in this capacity was investigated by constructing a badA hbaA double mutant. Although the double mutant grew more slowly on benzoate than badA cells, growth rates were still significant, suggesting the involvement of a third enzyme in benzoate activation. Competition experiments involving the addition of a small amount of cyclohexanecarboxylate to ligase assay mixtures implicated cyclohexanecarboxylate-coenzyme A ligase as being this third enzyme. These results show that wild-type R. palustris cells synthesize at least three enzymes that can catalyze the initial step in anaerobic benzoate degradation during growth on benzoate. This observation supports previous suggestions that benzoyl-coenzyme A formation plays a central role in anaerobic aromatic compound biodegradation.

Acyl Coenzyme A↗
PubMed1978

Biotyping of Serratia marcescens and its use in epidemiological studies.

A Serratia marcescens biotyping system using eight carbon sources (benzoate, DL-carnitine, m-erythritol, 3-hydroxybenzoate, 4-hydroxybenzoate, lactose, D-quinate, and trigonelline), a tetrathionate reduction test, production of prodigiosin, and horse blood hemolysis was derived from a recent numerical taxonomic study (Grimont et al., J. Gen. Microbiol. 98:39-66, 1977). A total of 98.6% of 2,210 isolates from various sources could be assigned to 1 of 19 biotypes. Distribution and spread of 1,088 S. marcescens isolates throughout 13 clinical departments of Pellegrin Hospital (Bordeaux, France) were studied from 1968 through 1975. Except for one that colonized the intestinal tract of newborns, the six pigmented biotypes were seldom isolated. Each of the 13 nonpigmented biotypes showed a particular pattern of distribution and spread. The usefulness of S. marcescens biotyping was shown by relating several isolates recovered from patients and their inanimate environment and by pointing out the possible existence of infections or colonizations by two unrelated biotypes. S. marcescens strains isolated from the natural environment (water) are usually pigmented, and their biotypes are uncommon in hospitals. Biotyping can, therefore, be of help in epidemiological and ecological surveys.

Bacteriological Techniques↗
PubMed1993

Potential for carboxylation-dehydroxylation of phenolic compounds by a methanogenic consortium.

An anaerobic consortium that carboxylated and dehydroxylated phenol to benzoate, and 2-cresol to 3-methylbenzoic acid, under methanogenic conditions was studied. Phenol induced this transformation activity. Addition of 4-hydroxypyridine or an increase in the concentration of proteose peptone to 0.5% (w/v) delayed the transformation. Phenol enhanced the rate of transformation of 2-cresol whereas 2-cresol delayed the transformation of phenol. Phenols with ortho-substitutions (chloro-, fluoro-, bromo-, hydroxyl-, amino-, or carboxyl-) were transformed to meta-substituted benzoic acids. However, meta- and para-substituted phenols (cresols, fluorophenols, and chlorophenols) were not transformed. Phenol was most rapidly metabolized, followed by catechol, 2-cresol, 2-fluorophenol, 2-aminophenol, 2-chlorophenol, 2-hydroxybenzoic acid, and 2-bromophenol. The consortium O-demethylated anisole to phenol and 2-methoxyphenol to catechol, and oxidized 2-hydroxybenzyl alcohol to 2-hydroxybenzoic acid. Aniline, 2-ethylphenol, 2-hydroxypyridine, 2-acetamidophenol, 2,6-dimethylphenol, 2-phenylphenol, and 1-naphthol were not metabolized.

Aminophenols↗
PubMed1995

Weak acid effects and fluoride inhibition of glycolysis by Streptococcus mutans GS-5.

Fluoride and a variety of other weak acids acted to reduce reversibily the acid tolerance of glycolysis by intact cells of Streptococcus mutans GS-5 as shown by higher final pH values in acid-drop experiments with glucose in excess. The order of effectiveness was fluoride > indomethacin > ibuprofen > ketoprofen > salicylate > sorbate > cinnamate > p-hydroxybenzoate > benzoate > ascorbate. Only fluoride also acted as an inhibitor of the glycolytic enzyme enolase. However, enolase in permeabilized cells was also inhibited by acidification with a sharp drop-off in activity between pH 6 and 5. It was proposed that the weak acids, including fluoride, acted to reduce glycolytic acid tolerance by enhancing cytoplasmic acidification and thereby inhibiting enzymes such as enolase. The potencies of the acids could not be predicted accurately from knowledge of pKa values, octanol-water partition coefficients, and molecular weights. It was concluded that their modes of action in acid sensitization involved perturbations of membrane function in addition to their acting as transmembrane carriers of protons. Methylparaben (methyl ester of p-hydroxybenzoate) was also a sensitizer but was less effective than the parent acid.

Acids↗
PubMed1999

Prolyl endopeptidase inhibitors from the underground part of Rhodiola sacra S. H. Fu.

Prolyl endopeptidase (PEP, EC 3.4.21.26) is an enzyme which plays a role in the metabolism of proline-containing neuropeptides, e.g., vasopressin, substance P and thyrotropin-releasing hormone (TRH), which have been suggested to be involved in learning and memory processes. In our systematic screening for PEP inhibitors from traditional Chinese medicines, we found that MeOH extract from the underground part of Rhodiola sacra S. H. Fu shows significant inhibitory activity against PEP from Flavobacterium meningosepticum. Examination of the constituents of the extract resulted in the isolation of nineteen known compounds, identified as hydroquinone (1), 4-hydroxybenzoic acid (2), caffeic acid (3), 4-hydroxycinnamic acid (4), suberic acid (5), protocatechuic acid (6), gallic acid (7), (-)-epigallocatechin 3-O-gallate (8), 2-phenylethyl beta-D-glucopyranoside (9), 3-O-galloylepigallocatechin-(4beta-->8)-epigallocatechin+ ++ 3-O-gallate (10), 2-phenylethyl alpha-L-arabinopyranosyl-(1-->6)-beta-D-glucopyranoside (11), sacranoside A (12), beta-D-glucopyranosyl 4-hydroxybenzoate (13), rhodiocyanoside A (14), rhodiooctanoside (15), sarmentosin (16), heterodendrin (17), arbutin (18) and 4-O-(beta-D-glucopyranosyl)-gallic acid (19). Among these, 1, 2, 5, 8-10, 13, 16, 18 and 19 have been isolated for the first time from R. sacra, among which 5, 9, 10, 13, 16, 18 and 19 have been isolated from Rhodiola plants for the first time. On the PEP inhibition, seven compounds (6-8, 10, 12, 18, 19) showed inhibition with an 1C50 of 27.8, 487, 1.47, 0.437, 348, 391 and 215 microM, respectively. The kinetic study of these inhibitors indicated that they are noncompetitive inhibitors, except for 6 which is a competitive inhibitor.

Drugs, Chinese Herbal↗