Only in Titles

           Search results for: PLP   

paperclip

#29349468   // Save this To Up

Absolute and relative-rate measurement of the rate coefficient for reaction of perfluoro ethyl vinyl ether (C2F5OCF[double bond, length as m-dash]CF2) with OH.

The rate coefficient (k1) for the reaction of OH radicals with perfluoro ethyl vinyl ether (PEVE, C2F5OCF[double bond, length as m-dash]CF2) has been measured as a function of temperature (T = 207-300 K) using the technique of pulsed laser photolysis with detection of OH by laser-induced fluorescence (PLP-LIF) at pressures of 50 or 100 Torr N2 bath gas. In addition, the rate coefficient was measured at 298 K and in one atmosphere of air by the relative-rate technique with loss of PEVE and reference reactant monitored in situ by IR absorption spectroscopy. The rate coefficient has a negative temperature dependence which can be parameterized as: k1(T) = 6.0 × 10-13 exp[(480 ± 38/T)] cm3 molecule-1 s-1 and a room temperature value of k1 (298 K) = (3.0 ± 0.3) × 10-12 cm3 molecule-1 s-1. Highly accurate rate coefficients from the PLP-LIF experiments were achieved by optical on-line measurements of PEVE and by performing the measurements at two different apparatuses. The large rate coefficient and the temperature dependence indicate that the reaction proceeds via OH addition to the C[double bond, length as m-dash]C double bond, the high pressure limit already being reached at 50 Torr N2. Based on the rate coefficient and average OH levels, the atmospheric lifetime of PEVE was estimated to be a few days.

2480 related Products with: Absolute and relative-rate measurement of the rate coefficient for reaction of perfluoro ethyl vinyl ether (C2F5OCF[double bond, length as m-dash]CF2) with OH.

Resorufin ethyl ether Glucose Assay With the La Anti beta3 AR Human, Poly Cultrex In Vitro Angiogen LSD 1 Fluorescent Assay k Methyltransferase G9a Ass Methyltransferase PRMT5 A Methyltransferase PRMT1 A Methyltransferase PRMT3 A Methyltransferase SUV39H1 Methyltransferase MLL Ass Methyltransferase EZH2 As

Related Pathways

paperclip

#29343643   // Save this To Up

Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, α-amino acid monooxygenase-decarboxylase.

Capuramycins are antimycobacterial antibiotics that consist of a modified nucleoside named uridine-5'-carboxamide (CarU). Previous biochemical studies have revealed that CarU is derived from UMP, which is first converted to uridine-5'-aldehyde in a reaction catalyzed by the dioxygenase CapA and subsequently to 5'-C-glycyluridine (GlyU), an unusual β-hydroxy-α-amino acid, in a reaction catalyzed by the pyridoxal-5'-phosphate (PLP)-dependent transaldolase CapH. The remaining steps that are necessary to furnish CarU include decarboxylation, O atom insertion, and oxidation. We demonstrate that Cap15, which has sequence similarity to proteins annotated as bacterial, PLP-dependent l-seryl-tRNA(Sec) selenium transferases, is the sole catalyst responsible for complete conversion of GlyU to CarU. Using a complementary panel of in vitro assays, Cap15 is shown to be dependent upon substrates O2 and (5'S,6'R)-GlyU, the latter of which was unexpected given that (5'S,6'S)-GlyU is the isomeric product of the transaldolase CapH. The two products of Cap15 are identified as the carboxamide-containing CarU and CO2 While known enzymes that catalyze this type of chemistry, namely α-amino acid 2-monooxygenase, utilize flavin adenine dinucleotide as the redox cofactor, Cap15 remarkably requires only PLP. Furthermore, Cap15 does not produce hydrogen peroxide and is shown to directly incorporate a single O atom from O2 into the product CarU and thus is an authentic PLP-dependent monooxygenase. In addition to these unusual discoveries, Cap15 activity is revealed to be dependent upon the inclusion of phosphate. The biochemical characteristics along with initiatory mechanistic studies of Cap15 are reported, which has allowed us to assign Cap15 as a PLP-dependent (5'S,6'R)-GlyU:O2 monooxygenase-decarboxylase.

1650 related Products with: Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, α-amino acid monooxygenase-decarboxylase.

2-Amino-5,6-dichloro-3(4H Anti Mouse asc type Amino Aspartyl aminopeptidase a Primary antibody GFR alp anti GFP antibody, rat mo 4-Amino-2,6-anhydro-3,4-d 3-Amino-N-[(4-chloropheny 2-Amino-5,6-dichloro-3(4H 4-[2-(2-Amino-4,7-dihydro 2-Amino-3-hydroxy-2-(hydr 4-Aminopiperidine-4-carbo Rabbit Anti-ASM Acid sphi

Related Pathways

  •  
  • No related Items
paperclip

#29343611   // Save this To Up

Structural insights into the catalytic mechanism of cysteine (hydroxyl) lyase from the hydrogen-sulfide producing oral pathogen, Fusobacterium nucleatum.

Hydrogen sulfide (H2S) plays important roles in the pathogenesis of periodontitis. Oral pathogens typically produce H2S from L-cysteine in addition to pyruvate and NH4+ However, fn1055 from Fusobacterium nucleatum subsp. nucleatum ATCC 25586 encodes a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the production of H2S and L-serine from L-cysteine and H2O, an unusual cysteine (hydroxyl) lyase reaction (β-replacement reaction). To reveal the reaction mechanism, the crystal structure of substrate-free Fn1055 was determined. Based on this structure, a model of the L-cysteine-PLP Schiff base suggested that the thiol group forms hydrogen bonds with Asp232 and Ser74, and the substrate α-carboxylate interacts with Thr73 and Gln147 Asp232 is a unique residue to Fn1055 and its substitution to asparagine (D232N) resulted in almost complete loss of β-replacement activity. The D232N structure obtained in the presence of L-cysteine contained the α-aminoacrylate-PLP Schiff base in the active site, indicating that Asp232 is essential for the addition of water to the α-aminoacrylate to produce the L-serine-PLP Schiff base. Rapid scan stopped-flow kinetic analyses showed an accumulation of the α-aminoacrylate intermediate during the reaction cycle, suggesting that water addition mediated by Asp232 is the rate-limiting step. In contrast, mutants containing substitutions of other active-site residues (Ser74, Thr73, and Gln147) exhibited reduced β-replacement activity by more than 100-fold. Finally, based on the structural and biochemical analyses, we propose a mechanism of the cysteine (hydroxyl) lyase reaction by Fn1055. This study leads to elucidation of the H2S-producing mechanism in F. nucleatum.

1319 related Products with: Structural insights into the catalytic mechanism of cysteine (hydroxyl) lyase from the hydrogen-sulfide producing oral pathogen, Fusobacterium nucleatum.

BACTERIOLOGY BACTEROIDES TCP-1 theta antibody Sour Recombinant Thermostable Recombinant Thermostable Recombinant Thermostable Recombinant Human PKC the Recombinant Human PKC the Recombinant Human PKC the Single Strand DNA Ligase, Single Strand DNA Ligase, Thermostable TDG Enzyme & Thermostable TDG Kit

Related Pathways

  •  
  • No related Items
paperclip

#29338677   // Save this To Up

Vitamin B-6 and depressive symptomatology, over time, in older Latino adults.

Low vitamin B-6 status has been linked to depressive symptomatology. We examined the longitudinal association of vitamin B-6 status with depressive symptomatology across 3-time points over ∼5-7 years in a cohort of older Hispanic adults.

2802 related Products with: Vitamin B-6 and depressive symptomatology, over time, in older Latino adults.

PI3-Kɣ Inhibitor, AS-605 PI3-Kɣ Inhibitor, AS-605 FAAH Inhibitor, PF-622 FAAH Inhibitor, PF-622; A FAAH Inhibitor, PF-622 FAAH Inhibitor, PF-622; A Androgen Receptor (Ab 650 Native Influenza A Virus Native Influenza A Virus Native Influenza A Virus Recombinant Influenza A V Recombinant Influenza A V

Related Pathways

paperclip

#29307827   // Save this To Up

Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae.

Pseudomonas syringae pv. tabaci ATCC 11528 produces tabtoxin, a β-lactam-containing dipeptide phytotoxin. Tabtoxinine-β-lactam (TβL), one of tabtoxin's constituent amino acids, structurally mimics lysine, and many of the proteins encoded by the tabtoxin biosynthetic gene cluster are homologs of lysine biosynthetic enzymes, suggesting that the tabtoxin and lysine biosynthetic routes parallel one another. We cloned and expressed TabB and TabD, predicted homologs of tetrahydrodipicolinate (THDPA)-N-acyltransferase and N-acyl-THDPA aminotransferase, respectively, to determine their activities in vitro. We confirmed that TabB succinylates THDPA and that TabD is a PLP-dependent aminotransferase that utilizes glutamate as an amine donor. Surprisingly, we also found that though TabD could utilize the TabB product N-succinyl-THDPA as a substrate, THDPA itself was also recognized. These observations reveal that TabB functionally duplicates DapD, the THDPA-N-succinyltransferase involved in lysine biosynthesis, and reinforce the close relationship between the metabolic logics underpinning the respective biosynthetic pathways.

1829 related Products with: Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae.

GLP 2 ELISA Kit, Rat Prog Anti 3 DG imidazolone Mon BYL-719 Mechanisms: PI3K- Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Mouse Anti P. aeruginosa Mouse Anti P.aeruginosa s

Related Pathways

  •  
  • No related Items
paperclip

#29300336   // Save this To Up

Characterization of a Potential Probiotic Lactobacillus brevis RK03 and Efficient Production of γ-Aminobutyric Acid in Batch Fermentation.

Lactic acid bacteria were isolated from fish and evaluated for their γ-aminobutyric acid (GABA)-producing abilities. Out of thirty-two isolates, Lactobacillus brevis RK03 showed the highest GABA production ability. The effects of various fermentation parameters including initial glutamic acid level, culture temperature, initial pH, and incubation time on GABA production were investigated via a singleparameter optimization strategy. For industrial large-scale production, a low-cost GABA producing medium (GM) broth was developed for fermentation with L. brevis RK03. We found that an optimized GM broth recipe of 1% glucose; 2.5% yeast extract; 2 ppm each of CaCO₃, MnSO₄, and Tween 80; and 10 μM pyridoxal phosphate (PLP) resulted in a maximum GABA yield of 62,523 mg/L after 88 h following the addition of 650 mM monosodium glutamate (MSG), for a conversion rate of 93.28%. Our data provide a practical approach for the highly efficient and economic production of GABA. In addition, L. brevis RK03 is highly resistant to gastric acid and bovine bile salt. Thus, the discovery of Lactobacillus strains with the ability to synthesize GABA may offer new opportunities in the design of improved health-promoting functional foods.

1837 related Products with: Characterization of a Potential Probiotic Lactobacillus brevis RK03 and Efficient Production of γ-Aminobutyric Acid in Batch Fermentation.

GST Inhibitor 2 (Ethacryn α-Acetamino-α-carboxy-( N-Acetyl-2-O-(5-bromo-1H- γ-Aminobutyric Acid C4H9 rac 3-Aminobutyric Acid C L-Aminobutyric Acid C4H9N L-Aminobutyric Acid-d3 C4 rac-2-Aminobutyric Acid-d L-2-Aminobutyric Acid Met L-2-Aminobutyric Acid-d5 DL-2-Aminobutyric Acid Me Aminomalonic Acid Bis(4-a

Related Pathways

paperclip

#29298733   // Save this To Up

Progressive striatonigral degeneration in a transgenic mouse model of multiple system atrophy: translational implications for interventional therapies.

Multiple system atrophy (MSA) is a rapidly progressive neurodegenerative disorder characterized by widespread oligodendroglial cytoplasmic inclusions of filamentous α-synuclein, and neuronal loss in autonomic centres, basal ganglia and cerebellar circuits. It has been suggested that primary oligodendroglial α-synucleinopathy may represent a trigger in the pathogenesis of MSA, but the mechanisms underlying selective vulnerability and disease progression are unclear. The post-mortem analysis of MSA brains provides a static final picture of the disease neuropathology, but gives no clear indication on the sequence of pathogenic events in MSA. Therefore, alternative methods are needed to address these issues. We investigated selective vulnerability and disease progression in the transgenic PLP-α-syn mouse model of MSA characterized by targeted oligodendroglial α-synuclein overexpression aiming to provide a neuropathological correlate of motor deterioration. We show progressive motor deficits that emerge at 6 months of age and deteriorate up to 18 months of follow-up. The motor phenotype was associated with dopaminergic cell loss in the substantia nigra pars compacta at 6 months, followed by loss of striatal dopaminergic terminals and DARPP32-positive medium sized projection neurons at 12 months. Olivopontocerebellar motor loops remained spared in the PLP-α-syn model of MSA. These findings replicate progressive striatonigral degeneration underlying Parkinson-variant MSA. The initiation of the degenerative process was linked to an increase of soluble oligomeric α-synuclein species between 2 and 6 months. Early region-specific α-synuclein-associated activation profile of microglia was found in MSA substantia nigra. The role of abnormal neuroinflammatory signalling in disease progression was further supported by increased levels of CD68, CCL3, CCL5 and M-CSF with a peak in aged PLP-α-syn mice. In summary, transgenic PLP-α-syn mice show a distinctive oligodendroglial α-synucleinopathy that is associated with progressive striatonigral degeneration linked to abnormal neuroinflammatory response. The model provides a relevant tool for preclinical therapeutic target discovery for human Parkinson-variant MSA.

2880 related Products with: Progressive striatonigral degeneration in a transgenic mouse model of multiple system atrophy: translational implications for interventional therapies.

Inflammation (Mouse) Quan Multiple lung carcinoma ( SensiTek HRP Anti-Mouse SensiTek HRP Anti-Mouse SensiTek Alk-Phos Anti-M UltraTek Alk-Phos Anti-M SensiTek HRP Anti-Mouse SensiTek Alk-Phos Anti-M UltraTek HRP Anti-Mouse UltraTek Alk-Phos Anti-M UltraTek HRP Anti-Mouse UltraTek HRP Anti-Mouse

Related Pathways

paperclip

#29294403   // Save this To Up

Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features.

Cellular metabolism of amino acids is controlled by a large number of pyridoxal 5'-phosphate (PLP) dependent enzymes. Diaminopropionate ammonia lyase (DAPAL), a fold type II PLP-dependent enzyme, degrades both the D and L forms of diaminopropionic acid (DAP) to pyruvate and ammonia. Earlier studies on the Escherichia coli DAPAL (EcDAPAL) had suggested that a disulfide bond located close to the active site may be crucial for maintaining the geometry of the substrate entry channel and the active site. In order to obtain further insights into the catalytic properties of DAPAL, structural and functional studies on Salmonella typhimurium DAPAL (StDAPAL) were initiated. The three-dimensional X-ray crystal structure of StDAPAL was determined at 2.5 Å resolution. As expected, the polypeptide fold and dimeric organization of StDAPAL is similar to those of EcDAPAL. A phosphate group was located in the active site of StDAPAL and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate (D-DAP). The unique disulfide bond of EcDAPAL was absent in StDAPAL, although the enzyme displayed comparable catalytic activity. Site directed mutagenesis of the cysteine residues involved in disulfide bond formation in EcDAPAL followed by functional and biophysical studies further confirmed that the disulfide bond is not necessary either for substrate binding or for catalysis. The activity of StDAPAL but not EcDAPAL was enhanced by monovalent cations suggesting subtle differences in the active site geometries of these two closely related enzymes.

1031 related Products with: Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features.

Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty Rabbit Anti-Salmonella ty

Related Pathways

  •  
  • No related Items
paperclip

#29277660   // Save this To Up

Properties and mechanism of d-glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d-amino acid specificity.

Salmonella enterica serovar Typhimurium utilizes a wide range of growth substrates, some of which are relatively novel. One of these unusual substrates is d-glucosaminate, which is metabolized by the enzymes encoded in the dga operon. d-Glucosaminate is transported and converted to d-glucosaminate-6-phosphate (G6P) by a phosphotransferase system, composed of DgaABCD. The protein product of dgaE, d-glucosaminate-6-phosphate ammonia lyase (DGL), converts G6P to 2-keto-3-deoxygluconate-6-phosphate, which undergoes a retroaldol reaction catalyzed by the DgaF protein to give d-glyceraldehyde-3-phosphate and pyruvate. We have now developed an improved synthesis of G6P which gives a higher yield. The DGL reaction is of mechanistic interest because it is one of only a few enzymes in the pyridoxal-5'-phosphate (PLP) dependent aminotransferase superfamily known to catalyze reaction of a d-amino acid substrate. The pH dependence of DGL shows an optimum at 7.5-8.5, suggesting a requirement for a catalytic base. α-Glycerophosphate and inorganic phosphate are weak competitive inhibitors, with Ki values near 30mM, and d-serine is neither a substrate nor an inhibitor. We have found in rapid-scanning stopped-flow experiments that DGL reacts rapidly with its substrate to form a quinonoid intermediate with λmax=480nm, within the dead time (ca. 2msec), which then rapidly decays (k=279s-1) to an intermediate with absorption between 330 and 350nm, probably an aminoacrylate complex. We suggest a mechanism for DGL and propose that the unusual stereochemistry of the DGL reaction requires a catalytic base poised on the opposite face of the PLP-substrate complex from the other members of the aminotransferase superfamily.

1100 related Products with: Properties and mechanism of d-glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d-amino acid specificity.

to PC4 (paired basic ami alanine-glyoxylate aminot Primary antibody GFR alp anti GFP antibody, rat mo AZD-3514 Mechanisms: Andr 4-Amino-2,6-anhydro-3,4-d 2-Amino-5,6-dichloro-3(4H 2-Amino-5,6-dichloro-3(4H Androst-4-ene-3,17-dion-1 Goat Anti- D-amino-acid o Anti Mouse asc type Amino CD40 Ligand protein CD40

Related Pathways

  •  
  • No related Items
paperclip


Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 218
#
Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 219
   // Save this To Up

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 243

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 243


Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 244

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 244

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 244

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 245

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 245


Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 251

2301 related Products with:


Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 255

Notice: Trying to get property of non-object in /home/genpcr5/public_html/gentaurpub.com/result.php on line 255
No related Items

Related Pathways

  •  
  • No related Items