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analysis
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in-gel detection of L-amino acid oxidase activity. L-amino acid concentrations in the range of 2-5 mM lead to activity bands of similar intensities, while higher concentrations results in partial substrate inhibition. Complete supplement mixture containing adenine, uracil, and L-amino acids (Arg, Asp, His, Ile, Leu, Lys, Met, Phe, Thr, Trp, Tyr, Val, each at different concentrations) is optimized at concentrations of 0.1-0.5% in combination with 1 and 2 mM o-phenylendiamine and horseradish peroxidase concentrations of 0.1-0.8 U/ml
drug development
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ACTX-6 demonstrates cytotoxicity in vitro and can inhibit tumor growth in vivo. It can markedly increase accumulation of sub-G1 phase, which suggests that this enzyme can induce apoptosis. ACTX-6 is a potential substance to develop into an antitumor drug
drug development
purified LAAO-I exhibits antiprotozoal activities which are demonstrated to be hydrogen-peroxide mediated. Exposure of promastigotes of Leishmania sp. results in dose-dependent parasite killing. LAAOs are interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potential as model for therapeutic agents
drug development
purified LAAO-I exhibits antiprotozoal activities which are demonstrated to be hydrogen-peroxide mediated. Exposure of promastigotes of Leishmania sp. results in dose-dependent parasite killing. LAAOs are interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potential as model for therapeutic agents
medicine
enzyme displays dosedependent inhibition on HIV-1 infection and replication
medicine
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antiviral (Dengue virus) and antiprotozoal (trypanocidal and leishmanicide) activities
medicine
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induces apoptosis in Hela cervical cancer cells in a concentration- and time-dependent manner. Caspase activation and PARP cleavage are involved in ACTX-8-induced apoptosis. ACTX-8 activates a mitochondrial pathway of apoptosis, which is regulated by Bcl-2 family members. Reactive oxygen species generated by ACTX-8 are involved in apoptosis. Translocation of Bax and Bad from the cytosol into mitochondria in ACTX-8-treated cells
medicine
LAAO does not induce platelet aggregation, but it has potent inhibitory activity on platelet aggregation induced by ADP and U46619. It shows no effect on platelet aggregation induced by thrombin, mucetin, ristocetin and stejnulxin
medicine
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LAAO-I exhibited bactericidal, antitumoral, trypanocidal, edematogenic, and platelet-aggregating activities. It induces typical apoptotic DNA fragmentation in HL-60 cells. Potential use of LAAO-I as a therapeutic agent for treatment of diseases in which induction of H2O2 production can be beneficial
medicine
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LAO decreases perfusion pressure, renal vascular resistance, glomerular filtration rate, sodium, potassium and chloride tubular reabsortion. Causes acute tubular necrosis foci
medicine
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LAO potently induces lesions in lungs and livers. LAO causes severe pneumorrhagia, pulmonary interstitial edema, fusion of pulmonary alveoli, cardiac interstitial edema and bleeding when being intravenously injected into BALB/c mice. Also induces liver cell necrosis and release of cytokines including IL-6, IL-12 and IL-2 from highly purified human peripheral blood monocytes and T cells, respectively. The ability of LAO will contribute to the understanding of the pathogenesis of snakebite wound
medicine
significantly inhibits Ehrlich ascites tumour growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of H2O2 from peritoneal macrophages. Later, LAAO-I induces mononuclear influx and peritoneal macrophage spreading. Animals treated with LAAO-I show higher survival time
medicine
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a high level of enzyme expression seems associated with absence of bone marrow involvement and better outcome in follicular lymphoma cases, enzyme levels could serve as prognosis factor
medicine
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the antibacterial activity of the enzyme is similar to that of kanamycin
medicine
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the enzyme does not exhibit cytotoxic activities against erythrocytes and peripheral blood mononuclear cells but causes cytotoxicity on several cancer cell lines and induces platelet aggregation in dose-dependent manner. Furthermore, the enzyme shows remarkable effect against Gram-positive and Gram-negative bacteria
medicine
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the enzyme has a strong selective cytotoxic activity on tumor cell lines (JURKAT, SK-BR-3 and B16F10)
medicine
the enzyme is a potential tool to instigate antiapoptotic protein regulation that contributes to drive chronic myeloid leukemia therapy
medicine
after infection with Cryptocaryon irritans, the LAAO mRNA is upregulated early post infection (from 6 to 24 h) in both gill and spleen, but then returns to normal levels
medicine
apotxin can selectively kill tumor cells, with less cytotoxicity to the normal cells. Its anti-tumor activity is mainly due to the hydrogen peroxide produced from LAAO oxidation, but catalase does not reverse its anti-tumor effect completely. Deglycosylation can significantly reduce the LAAO activity and anti-tumor activity of apotxin
medicine
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coadministering adipose-derived mesenchymal stromal cells and Ophiophagus hannah L-amino acid oxidase in a mouse model of methicillin-resistant Staphylococcus aureus-infected wounds results in reduction of MRSA load by one order of magnitude to the approximate range of 6 log10 colony-forming units compared to untreated controls (7.3 log10 CFU). Similar wound healing and improvements in histological parameters are observed between the two groups. Coadministration of adipose-derived mesenchymal stromal cells and L-amino acid oxidase reduces bacterial burden by approximately two orders of magnitude to 5.1 log10 CFU and leads to a significant enhancement in the wound healing process
medicine
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enzyme displays fibrinogen polymerizing procoagulation and PMSF-associated anticoagulation. The LAAO must be polymerizing fibrinogen independent of endogenous thrombin generation and FXIII crosslinking. The direct deaminating action of LAAO, not the coincident generation of H2O2, is responsible for the coagulation procoagulant profile
medicine
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LAAO exhibits a considerable cytotoxic activity against breast cancer cell line MCF-7 with IC50 value of 2.75 microg/ml. LAAO triggers antiproliferative activity via extensive H2O2 generation. LAAO exhibits a significant bactericidal activity against gram-positive and gram-negative bacteria, particularly Staphylococcus aureus and Escherichia coli with MIC values of 20 microg/ml
medicine
LAAO is involved in dermonecrosis in mice and shows cytotoxic effects in normal human keratinocytes, the major cell type in the epidermis, which undergoes extensive necrosis at the snakebite site. Pharmacological inhibition by N-acetyl cysteine prevents Bothrops atrox venom-induced necrosis. Treatment with purified LAAO decreases keratinocyte viability with an effective Concentration (EC50) of 5.1 microg/ml. Cytotoxicity caused by LAAO is mediated by H2O2 and treated cells undergo autophagy, followed by apoptosis and necrosis. LAAO induces morphological alterations that precede cell death
medicine
the enzyme exhibits cytotoxicity against fibroblast cell line and kills Leishmania amazonensis promastigotes, intensified by substrate addition
medicine
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the antibacterial activity of the enzyme is similar to that of kanamycin
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synthesis
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use of enzyme as a catalyst in supercritical CO2. enzyme activity increases after exposure to supercritical conditions by up to 15%. Enzyme is more stable in supercritical CO2 than under atmospherical pressure, and oxidation of 3,4-dihydroxyphenyl-L-Ala is best under supercritical conditions
synthesis
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engineering Escherichia coli to produce phenylpyruvate. Knock-out of three aminotransferases increases the phenylpyuvate titer from 3.3 to 3.9 g/l and the substrate conversion ratio to 97.5%. The L-amino acid deaminase triple mutant D165K/F263M/L336M produces 10.0 g phenylpyruvate per l, with a substrate conversion ratio of 100%. An optimal fed-batch biotransformation process gives 21 g phenylpyruvate per l within 8 h
synthesis
expression of isoform LAOO4 in the yeast Pichia pastoris with a 9His-tag and comparison with the 6His-LAAO4 expressed in Escherichia coli. The expression of the enzyme with an ER-signal sequence in Pastoris pastoris results in a glycosylated, secreted protein. The enzymatic activity without activation is higher after expression in Pichia pastoris compared to Escherichia coli. Due to treatment with acidic pH, a striking increase of activity can be detected for both expression systems resulting in similar specific activities after acid activation
synthesis
purified aldehyde-tagged 6His-hcLAAO4 is covalently bound to a hexylamine resin via the Calpha-formylglycine residue. The immobilized enzyme can be reused repeatedly to generate phenylpyruvate from L-phenylalanine with a total turnover number of 17600 and is stable for over 40 days at 25 °C
synthesis
synthesis of phenylpyruvic acid from L-phenylalanine using biotransformations with specified amounts of purified enzyme or activated lysate prepared from the whole cells. 20 mM of substrate are converted after 4 h reaction. The formation of undesired byproducts such as phenylacetic acid is suppressed using a commercially available catalase enzyme
synthesis
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engineering Escherichia coli to produce phenylpyruvate. Knock-out of three aminotransferases increases the phenylpyuvate titer from 3.3 to 3.9 g/l and the substrate conversion ratio to 97.5%. The L-amino acid deaminase triple mutant D165K/F263M/L336M produces 10.0 g phenylpyruvate per l, with a substrate conversion ratio of 100%. An optimal fed-batch biotransformation process gives 21 g phenylpyruvate per l within 8 h
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additional information
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a helical domain is exclusively responsible for the unusual dimerisation mode of the enzyme and is not found in other members of the family so far. Most groups present at the active site are involved in substrate recognition, binding and fixation, i.e. they direct the trajectory of the interacting orbitals. In this mode of catalysis orbital steering/interactions are the predominant factors for the chemical step(s). A mirrorsymmetrical relationship between the two substrate-binding sites of D and L-amino acid oxidases is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the residues in the active site
additional information
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expressed LAAO exhibits the same electrophoretic mobility as native LAAO and exhibits approximately the same extent of glycosylation as authentic LAAO from snake venom. Catalytic properties and substrate specificity of recombinant LAAO are similar to those of native enzyme
additional information
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LAAO causes cell death by induction of apoptosis in yeast. Lower concentrations of hydrogen peroxide accompanied by leucine deficiency may have a role in enhancing cell death in leucine auxotrophic yeast strain. LAAO interacts with the cell surface of yeast. Depletion of leucine from the medium by LAAO and the interaction of LAAO with yeast cells are shown to be the major factors responsible for cell demise in the presence of catalase
additional information
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LAAO contributes to competitive edge of Streptococcus oligofermentans over Streptococcus mutans in mixed-species biofilm with peptone
additional information
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LAAO dose-dependently induces aggregation of washed human platelets. It induces tyrosine phosphorylation of a number of platelet proteins including Src kinase, spleen tyrosine kinase, and phospholipase C gamma2. Both H2O2 production and binding to platelet membrane proteins may be involved in its action. The enzyme binds to the platelet membrane to enhance the sensitivity of platelets to H2O2. At the same time, H2O2 released by the enzyme activates platelets by an unknown mechanism
additional information
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LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity
additional information
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LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
additional information
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LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
additional information
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LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
additional information
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LAO is involved in the innate immunity of fish skin. Shows potent antibacterial activity against fish pathogens, specifically Gram-negative bacteria such as Aeromonas hydrophila, Aeromonas salmonicida and Photobacterium damselae ssp. piscicida
additional information
LAO is involved in the innate immunity of fish skin. Shows potent antibacterial activity against fish pathogens, specifically Gram-negative bacteria such as Aeromonas hydrophila, Aeromonas salmonicida and Photobacterium damselae ssp. piscicida
additional information
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potent and effective activity of SSAP against waterborne virulent pathogens. Shows antibacterial activity, acts selectively on Gram-negative bacteria. SSAP inhibits potently the growth of Aeromonas salmonicida, Photobacterium damselae subsp. piscicida and Vibrio parahaemolyticus with a minimum inhibitory concentration of 0.078, 0.16 and 0.63 microg/mL, respectively. Bacteria binding activity may be involved in the bacterial cell selectivity of SSAP. Treatments with SSAP induce cell surface damage to Aeromonas salmonicida, remarkable elongation of Photobacterium damselae subsp. piscicida bodies and pores into Vibrio parahaemolyticus cells
additional information
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SSAP is predominantly synthesized in skin and gill and probably functions as an antibacterial LAO in both tissues. It shows antibacterial activity against Photobacterium damselae subsp. piscicida
additional information
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the enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. LAAO dose-dependently inhibits ADP- or collagen-induced platelet aggregation with IC50 of 0.094 micromol and 0.036 micromol, respectively
additional information
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LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
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additional information
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LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity
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additional information
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LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity
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additional information
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LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity
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additional information
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LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
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