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At least 19 recordsLinked to original sources
PubMed2026

Unraveling cadaverine toxicity effect to guide the engineering of robust strain.

End-product inhibition represents a major challenge in the microbial synthesis of various value-added chemicals. Cadaverine, a key monomer for polyamide synthesis, exhibits severe cytotoxicity, limiting its high-titer biosynthesis. Here, transcriptomic analysis and genome-wide library screening were integrated to systematically elucidate the cytotoxic mechanisms of cadaverine in Escherichia coli (E. coli) and identify beneficial genes for enhanced tolerance and overproduction. Transcriptomic analysis revealed that high concentrations of cadaverine disrupted cell membrane integrity and impaired oxidative phosphorylation, leading to redox imbalance and reactive oxygen species (ROS) accumulation. Subsequent genome-wide screening further confirmed these toxicity mechanisms and uncovered crucial cellular defense strategies. Functional validation highlighted the important role of NikR, UbiE, and YcbX in enhancing membrane integrity, restoring respiratory function and ROS homeostasis, or scavenging 6-N-hydroxylaminopurine (6-HAP) to prevent DNA damage. Among these, YcbX emerged as the most effective target for improving production. Consequently, we constructed a robust E. coli strain by implementing a dynamic regulation system for YcbX expression under cadaverine-responsive promoters, which significantly enhanced cadaverine biosynthesis to 87.2 g/L (a 46.8% enhancement). This work provides an in-depth understanding of cadaverine toxicity and tolerance, offering valuable targets and strategies for the rational design of high-performance microbial cell factories for diamines.

6-HAP clearance↗
PubMed1979

Formation of cadaverine in the pregnant rat.

The formation as well as the content of cadaverine were determined in different tissues of pregnant and non-pregnant rats. The placenta and ovary were most potent in the ability to form cadaverine. To our knowledge this is the first report of an in vitro formation of cadaverine linked to a normal physiological process, i.e. pregnancy. The highest concentration of cadaverine was found in the placenta and ovary of the pregnant rat. Treatment with aminoguanidine generally elevated the content of cadaverine, indicating a role of diamine oxidase as a regulator of diamine content.

Amine Oxidase (Copper-Containing)↗
PubMed1976

Biosynthesis of cadaverine in mice under the influence of an anabolic steroid.

The content of cadaverine (1,5-diaminopentane) in the kidney and urine was investigated in mice treated with the anabolic steroid Durabolin (nondrolone phenpropionate). After administration of this steroid cadaverine was found in the kidneys, whereas this amine could not be detected in the kidney of controls. The urinary excretion of cadaverine was elevated 50 times after Durabolin administration. An enzyme catalyzing the formation of cadaverine from lysine was shown for the first time to be present in mammalian tissue, namely in the kidney of mice after Durabolin administration.

Animals↗
PubMed1978

[Cadaverine is an intermediate in the biosynthesis of arthrobactin and ferrioxamine E (author's transl)].

Cadaverin was more readily incorporated than lysine into arthrobactin from Arthrobacter pascens and into ferrioxamin E from Streptomyces glaucescens. From a racemic mixture only the L-isomer of lysine is incorporated. The L-lysine decarboxylase activity was measured in vivo and in vitro. The enzyme from Arthrobacter pascens is not inducable by lysine and completely repressed by 5.10(-6) M Fe3+. In Klebsiella pneumoniae, the producer of aerobactin, only a very low activity of L-lysine decarboxylase was detected.

Arthrobacter↗
PubMed1975

A re-examination of the cleavage of fibrinogen and fibrin by plasmin.

Three Fragment D species (D1, D2, D3) were isolated with time from a plasmin digest of fibrinogen and had molecular weights of 92,999, 86,000 and 82,000 by summation of subunit molecular weights from sodium dodecyl sulfate polyacrylamide gel electrophoresis. Their molecular weights by sedimentation equilibrium ultracentrifugation were 94,000 t87,000, 88,000 to 82, 000, and 76,000 to 70,000 depending on the values calculated for the partial specific volumes. Each of the Fragment D species contained three disulfide-linked subunits derived from the Aalpha, Bbeta, and gamma chains of fibrinogen and differed only in the extent of COOH-terminal degradation of their gamma chain derivatives. Plasmin cleaved Fragment D1 to release the cross-link sites from its gamma' subunit of 38,000 molecular weight; however, the beta'' subunit of 42,000 molecular weight and the alpha'' subunit of 12,000 molecular weight were resistant to further digestion by plasmin. Fragment D isolated from highly cross-linked fibrin had a dimeric structure due to cross-link formation between the gamma' subunits of two fibrinogen Fragment D species. The molecular weight of fibrin Fragment D was 184,000 by summation of subunit molecular weights and 190,000 to 175,000 by sedimentation equilibrium. Cross-linking the gamma chain, as well as incorporating the site-specific fluorescent label monodansyl cadaverine into the gamma chain cross-link acceptor site, prevented its COOH-terminal degradation by plasmin. Therefore, only one species of fibrin Fragment D, as well as only one species of monodansyl cadaverine-labeled fibrin Fragment D monomer, was generated during plasmin digestion. These results show unequivocally that each fibrinogen Fragment D contains only three subunit chains and therefore the digestion of fibrinogen by plasmin must result in the production of two Fragment D molecules from each fibrinogen molecule. The recently proposed model of fibrinogen cleavage that postulates the generation of a single Fragment D with three pairs of subunit chains from each fibrinogen molecule is incorrect. Incorporation of monodansyl cadaverine into the cross-link acceptor sites of the alpha chain did not alter its cleavage by plasmin detectably. A series of monodansyl cadaverine-labeled peptides, which ranged in molecular weight from 40,000 to 23,000, were cleaved from the alpha chain of monodansyl cadaverine-labeled fibrin monomer during the early stages of plasmin digestion. These peptides were degraded progressively to a brightly fluorescent plasmin-resistant peptide of 21,000 molecular weight and a weakly fluorescent peptide of 2,500 molecular weight. Thus both alpha chain cross-link acceptor sites are contained within a peptide segment of 23,000 molecular weight.

Amino Acids↗
PubMed1977

Catabolism of L-lysine by Pseudomonas aeruginosa.

Pseudomonas aeruginosa PACI grows poorly on L-lysine as sole source of carbon but mutant derivatives which grow rapidly were readily isolated. Studies with one such mutant, P. aeruginosa PAC586, supported the existence of a route for L-lysine catabolism which differes from those reported previously in other species of Pseudomonas. The postulated route, the cadaverine or decarboxylase pathway, is initiated by the decarboxylation of L-lysine and involves the following steps: L-lysine leads to cadverine leads to I-piperideine leads 5-aminovalerate leads to glutarate semialdehyde leads glutarate. Evidence for this pathway is based on the characterization of the pathway reactions and the induction of the corresponding enzymes by growth on L-lysine. The first three enzymes were also induced by growth on cadaverine and to a lesser extent by 5-aminovalerate. No evidence was obtained for the presence of pathways involving L-lysine 2-monooxygenase or L-pipecolate dehydrogenase, but another potential route for L-lysine catabolism initiated by L-lysine 6-aminotransferase was detected. Studies with mutants unable to grow on L-lysine supported the existence of more than one catabolic pathway for L-lysine in this organism and indicated that all routes converge on a pathway for glutarate catabolism which generates acetyl-CoA. Pipecolate catabolism also appeared to converge on the glutarate pathway in P. AERUGINOSA. The results suggested that the growth rate of the parental strain is limited by the rate of transport and/or decarboxylation of L-lysine. The cadaverine pathway was present, but not so highly induced, in the parental strain P. aeruginosa PACI. Pseudomonas fluorescens contained enzymes of both the cadaverine (decarboxylase) and oxygenase pathways, strains of P. putida (biotypes A and B) contained enzymes of the oxygenase pathway but not the decarboxylase pathway and P. multivorans appeared deficient in both. All these species possessed L-lysine aminotransferase activity.

Cadaverine↗
PubMed2025

Loss of responses to odorants and pheromones in mPRγ (paqr5b)-knockout zebrafish.

In our previous study, we generated a membrane-type progesterone receptor γ (paqr5b) knockout zebrafish line. Knocking out paqr5b by genome editing resulted in the loss of neurons in the olfactory rosette (OR). These findings indicated that Paqr5b plays an essential role in the formation of olfactory neurons. In this study, we investigated the extent to which paqr5b-/- fish lacking olfactory neurons retain their sense of smell. We used a reported tank for zebrafish olfactory analysis with a dividing plate in the middle. The tank was divided into three zones: the right zone, where test substances were added; the neutral zone; and the left zone. The fish were released into the neutral zone at the beginning of each test, the chemical was added to the corner of the right zone, and a 3-min video was taken to track the movements of the fish. The video was then played back, and the time spent in the three zones was counted manually. Both male and female paqr5b+/+ and paqr5b-/- zebrafish were separately analyzed for time spent in the three zones after exposure to ATP, cadaverine, and the pheromone 17α,20β-dihydroxy-4-pregnen-3-one (DHP). Both male and female paqr5b+/+ zebrafish were strongly attracted to ATP and stayed in the right zone for approximately 2 min (67%). In addition, paqr5b+/+ zebrafish avoided cadaverine and stayed longer in the left zone than in any other zone. In contrast, paqr5b-/- zebrafish stayed in all three zones for approximately the same amount of time, even after exposure to ATP and cadaverine. The paqr5b+/+ fish were attracted to DHP and stayed in the right zone longer. Paqr5b-/- zebrafish of either sex were not reactive to DHP exposure. These results showed that paqr5b-/- zebrafish lacking olfactory neurons lost responsiveness to odorants and pheromones.

Animals↗
PubMed1976

Isolation, purification and characterization of bovine epidermal transglutaminase.

A crosslinking enzyme, epidermal transglutaminase, was isolated from soluble proteins of glabrous cow snout epidermis. This enzyme stabilized fibrin clots rendering them insoluble in 2% acetic acid. It also catalyzed the incorporation of the fluorescent amine, dansyl cadaverine, into casein. Epidermal transglutaminase was purified by chromatography upon DEAE-Sephadex A-50, zone electrophoresis in Pevikon, and Sephadex G-200 gel permeation chromatography. The highly purified substance, which had a specific activity of 3267 amine-incorporating units/mg per h and a molecular weight of 55000, behaved as a single molecular species in the analytical ultracentrifuge. It had a sedimentation coefficient of 4.4 S and migrated as a gamma-globulin at pH 8.6; it displayed anomalous migration in polyacrylamide gels containing sodium dodecyl sulfate. The enzyme was dependent upon free calcium ions and a reduced sulfhydryl group for activity. The apparent Km for dansyl cadaverine was 1.2 - 10(-4) at pH 7.5. Monospecific antiserum to bovine epidermal transglutaminase precipitated with the enzyme in agar. The antiserum prevented fibrin crosslinking but enhanced incorporation of dansyl cadaverine into casein by the enzyme. The epidermal enzyme differed biochemically and immunochemically from bovine plasma transglutaminase (Factor XIII).

Animals↗
PubMed1975

Plasmic degradation of human fibrinogen. IV. Identification of subunit chain remnants in fragment Y.

A method is presented for detection of cross-linking acceptor sites on fibrinogen chains, using monodansyl-cadaverine labeling in the presence of activated fibrin stabilizing factor, and polyacrylamide electrophoresis in the presence of sodium dodecyl sulfate. Fluorescent gamma-chain monomers and dimers were produced at a considerably faster rate than the labeled alpha-chain derivative. Purified fragments X, Y and D were prepared all from the same plasmic digest of fibrinogen. Following incubation with fibrin stabilizing factor, thrombin and monodansyl-cadaverine, they were reduced with beta-mercaptoethanol and examined by sodium dodecyl sulfate/acrylamide electrophoresis. Three gamma-chains (mol. wts 49 000, 42 000 and 39 000) had reacted with dansyl-cadaverine while no alpha-chain remnant took up the label. Additional protein and carbohydrate staining further facilitated identification of the individual subunit chains. At least three critical peptide bonds, located on alpha, beta- and gamma-chain remnants, must be broken during conversion of fragment Y into D and E. Sequential cleavage results in heterogeneous appearance of reduced subunit chains. As a consequence, there exist several molecular entities of fragment Y, all of which may have the same molecular weight though they represent various products of progressive plasmic digestion. Our results are compatible with the model of asymmetric degradation of fibrinogen, according to which fragment X produces 1 mol of fragment E e and 2 mol of the monomeric fragment D.

Amino Acid Sequence↗
PubMedDate not supplied

A model mechanism for the enzymatic synthesis of lupin alkaloids.

A crude enzyme preparation obtained from cell suspension cultures of Lupinus polyphyllus catalyzes the pyruvate dependent conversion of cadaverine into the tetracyclic lupin alkaloids. As the first reaction product 17-oxosparteine could be identified by gas-liquid chromatography and mass spectroscopy. In some experiments sparteine was found additionally. A participation of diamine oxidase could be ruled out. The cadaverine-pyruvate transaminating enzyme system (17-oxosparteine synthase) catalyzes the formation of 17-oxosparteine from three cadaverine units without releasing free intermediates. These results are inconsistent with the hypothetical mechanism thus far formulated for the lupin alkaloid biosynthesis. A new enzymatic model mechanism is proposed regarding both the results of the enzymatic experiments and those of the in vivo tracer studies.

Alkaloids↗
PubMed1977

Gas chromatography mass spectrometry analysis of polyamines using deuterated analogs as internal standards.

Quantitative analyses of subnanomole quantities of the polyamines putrescine, cadaverine, spermidine and spermine by the gas chromatography mass spectrometry technique of selected ion monitoring are complicated by effects of the chromatographic column. These effects include sample retention by the column and chromatographic band broadening, and are sufficiently serious that spermine (as the trifluoroacetylated derivative) was not detectable at levels below 50 picomoles. Because the chromatographic behaviors of the four polyamines vary, quantiative analysis using a single internal standard is not feasible. The deuterated polyamine analogs, putrescine-2H4, cadaverine-2H4, spermidine-2H6 and spermine-2H8, have been synthesized and used to accomplish quantiative analyses of the corresponding isotopically natural abundance polyamines to the one picomole level. This enhancement in analytical sensitivity is accomplished by use of large excesses (greater than or equal to 100 picomoles) of the deuterated analogs to improve chromatographic band profiles. The use of such large molar excesses of deuterated analogs for selected ion monitoring analyses is possible because their electron impact spectra exhibit high mass ions ([M-F3C]+, [M-F3CCO]+) which possess greater than or equal to 4 deuterium atoms and have intensity ratios (I2H(max):IH) of 500 or greater.

Cadaverine↗
PubMed1978

Enhancement of thermal killing by polyamines. II. Uptake and metabolism of exogenous polyamines in hyperthermic Chinese hamster cells.

The uptake and metabolism of the polyamines spermine, spermidine, cadaverine and putrescine, previously shown to potentiate heat sensitivity, were studied in cultured Chinese hamster cells. Heat (42 degrees C) causes enhanced uptake of exogenously supplied polyamines into the acid-soluble fraction of the cells. Putrescine is taken up exceptionally fast at 37 degrees C, about 10 times faster than its homologue, cadaverine. This uptake is slower at 42 degrees C. The polyamines taken up were metabolized to some extent and the metabolites were similar at 37 degrees C and 42 degrees C except in the case of putrescine. These results suggest that potentiation of heat-sensitivity is probably mediated by the polyamines as such and not by their metabolites. Polyamines slightly protect the cells against the inhibitory effect of heat on RNA and protein synthesis. It is suggested that exogenous polyamines interact with nucleic acids inside the cell, and this interaction may underlie their synergism with heat. The exact nature of this interaction and the way it leads to enhanced thermal sensitivity are still obscure.

Animals↗
PubMed1975

Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography.

The present study describes the use of affinity chromatography to achieve a high degree of purification of histaminase (diamine oxidase, EC 1.4.3.6) from plasma of women in the third trimester of pregnancy. The procedure is based upon the binding of histaminase to cadaverine, a diamine substrate for the enzyme, which is coupled to Sepharose. Contaminant proteins were removed by high concentrations of NaCl (up to 1.0M), and the histaminase was then eluted from the column with a buffer containing 300--400 units/ml of sodium heparin. The purification technique has the following characteristics: (1) in optimal experiments, 3000-fold purification of enzyme was obtained; (2) the yield of enzyme was as great as 25%; (3) the binding of histaminase to the amine groups of the cadaverine appears to represent a true "affinity" phenomenon since enzyme bound to DEAE-cellulose under neutral pH conditions was eluted at much lower concentrations of NaCl (less than 0.4 M). The enzyme purified by the present procedure has the following properties: (1) disc gel polyacrylamide electrophoresis showed two protein bands for 1000--3000-fold pure histaminase; the major band may represent a contaminant protein, while the minor band corresponded to the position of histaminase activity; (2) a 90 000 molecular weight subunit for the plasma histaminase was identified on calibrated sodium dodecyl sulfate gels; this value agrees well with previous estimations for the subunit size of human placental histaminase; (3) the purified enzyme behaved as classical histaminase (diamine oxidase) in that it was totally inhibited by low concentrations of aminoguanidine, but was less inhibited by semicarbazide and by inhibitors of monoamine oxidase, and the enzyme was active against histamine and putrescine, but not against the monoamines benzylamine and tryptamine. Also, the enzyme was strongly inhibited by NaCl.

Amine Oxidase (Copper-Containing)↗
PubMed1979

Decarboxylation of ornithine and lysine in rat tissues.

The possibility that arginine and lysine might be decarboxylated by rat tissues was investigated. No evidence for decarboxylation of arginine could be found. Lysine decarbosylase (L-lysine carboxy-lyase, EC 4.1.1.18) activity producing CO2 and cadaverine was detected in extracts from rat ventral prostate, androgen-stimulated mouse kidney, regenerating rat liver and livers from rats pretreated with thioacetamide. These tissues all have high ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activities. Lysine and ornithine decarboxylase activities were lost to similar extents on inhibition of protein synthesis by cycloheximide and on exposure to alpha-difluoromethylornithine. A highly purified ornithine decarboxylase preparation was able to decarboxylate lysine and the ratio of ornithine to lysine decarboxylase activities was constant throughout purification. Kinetic studies of the purified preparation showed that the V for ornithine was about 4-fold greater than for lysine, but the Km for lysine (9 mM) was 100-times greater than that for ornithine (0.09 mM). These experiments indicate that all of the detectable lysine decarboxylase activity in rat and mouse tissues was due to the action of ornithine decarboxylase and that significant cadaverine production in vivo would occur only when ornithine decarboxylase activity is high and lysine concentrations substantially exceed those of ornithine.

Animals↗