107-95-9Relevant articles and documents
Mechanism of cysteine-dependent inactivation of aspartate/glutamate/ cysteine sulfinic acid α-decarboxylases
Liu, Pingyang,Torrens-Spence, Michael P.,Ding, Haizhen,Christensen, Bruce M.,Li, Jianyong
, p. 391 - 404 (2013)
Animal aspartate decarboxylase (ADC), glutamate decarboxylase (GDC) and cysteine sulfinic acid decarboxylase (CSADC) catalyze the decarboxylation of aspartate, glutamate and cysteine sulfinic acid to β-alanine, γ-aminobutyric acid and hypotaurine, respectively. Each enzymatic product has been implicated in different physiological functions. These decarboxylases use pyridoxal 5-phosphate (PLP) as cofactor and share high sequence homology. Analysis of the activity of ADC in the presence of different amino determined that beta-alanine production from aspartate was diminished in the presence of cysteine. Comparative analysis established that cysteine also inhibited GDC and CSADC in a concentration-dependent manner. Spectral comparisons of free PLP and cysteine, together with ADC and cysteine, result in comparable spectral shifts. Such spectral shifts indicate that cysteine is able to enter the active site of the enzyme, interact with the PLP-lysine internal aldimine, form a cysteine-PLP aldimine and undergo intramolecular nucleophilic cyclization through its sulfhydryl group, leading to irreversible ADC inactivation. Cysteine is the building block for protein synthesis and a precursor of cysteine sulfinic acid that is the substrate of CSADC and therefore is present in many cells, but the presence of cysteine (at comparable concentrations to their natural substrates) apparently could severely inhibit ADC, CSADC and GDC activity. This raises an essential question as to how animal species prevent these enzymes from cysteine-mediated inactivation. Disorders of cysteine metabolism have been implicated in several neurodegenerative diseases. The results of our study should promote research in terms of mechanism by which animals maintain their cysteine homeostasis and possible relationship of cysteine-mediated GDC and CSADC inhibition in neurodegenerative disease development.
Photocatalytic One-Step Syntheses of Cyclic Imino Acids by Aqueous Semiconductor Suspensions
Ohtani, Bunsho,Tsuru, Shigeto,Nishimoto, Sei-ichi,Kagiya, Tsutomu
, p. 5551 - 5553 (1990)
Optically active cyclic imino acids, pipecolinic acid and proline, are readily obtained from α,ω-diamino carboxylic acids and their Nω-substituted derivatives by the photoirradiation of aqueous suspensions of TiO2 or CdS loaded with platinum oxides under Ar at room temperature.
Abiotic Synthesis of Amino Acids by Proton Irradiation of a Mixture of Carbon Monoxide, Nitrogen, and Water
Kobayashi, Kensei,Oshima, Tairo,Yanagawa, Hiroshi
, p. 1527 - 1530 (1989)
We have shown that proton irradiation simulating the action of cosmic rays and solar flare particles formed proteinous and non-proteinous amino acids such as glycine, alanine, aspartic acid and β-alanine from a mixture of carbon monoxide, carbon dioxide, nitrogen and water.The yield of amino acids per unit energy was the highest obtained among various prebiotic energy sources used.This result suggests the possibility of the formation of amino acids mildly reduced primitive atmospheres on the earth.
Mass spectrometry assay for studying kinetic properties of dipeptidases: Characterization of human and yeast dipeptidases
Pandya, Vaibhav,Ekka, Mary Krishna,Dutta, Rajesh Kumar,Kumaran
, p. 134 - 142 (2011)
Chemical modifications of substrate peptides are often necessary to monitor the hydrolysis of small bioactive peptides. We developed an electrospray ionization mass spectrometry (ESI-MS) assay for studying substrate distributions in reaction mixtures and determined steady-state kinetic parameters, the Michaelis-Menten constant (Km), and catalytic turnover rate (V max/[E]t) for three metallodipeptidases: two carnosinases (CN1 and CN2) from human and Dug1p from yeast. The turnover rate (V max/[E]t) of CN1 and CN2 determined at pH 8.0 (112.3 and 19.5 s-1, respectively) suggested that CN1 is approximately 6-fold more efficient. The turnover rate of Dug1p for Cys-Gly dipeptide at pH 8.0 was found to be slightly lower (73.8 s-1). In addition, we determined kinetic parameters of CN2 at pH 9.2 and found that the turnover rate was increased by 4-fold with no significant change in the Km. Kinetic parameters obtained by the ESI-MS method are consistent with results of a reverse-phase high-performance liquid chromatography (RP-HPLC)-based assay. Furthermore, we used tandem MS (MS/MS) analyses to characterize carnosine and measured its levels in CHO cell lines in a time-dependent manner. The ESI-MS method developed here obviates the need for substrate modification and provides a less laborious, accurate, and rapid assay for studying kinetic properties of dipeptidases in vitro as well as in vivo.
Artificial trinuclear metallopeptidase synthesized by cross-linkage of a molecular bowl with a polystyrene derivative
Moon, Sung-Ju,Jeon, Joong Won,Kim, Heesuk,Suh, Myunghyun Paik,Sun, Junghun
, p. 7742 - 7749 (2000)
A novel methodology is reported for construction of active sites of artificial multinuclear metalloenzymes: Transfer of metal-chelating sites confined in a prebuilt cage to a polymeric backbone. Artificial active sites comprising two or three moieties of Cu(II) complex of tris(2-aminoethyl)amine (tren) were prepared by transfer of Cu(II)tren units confined in a molecular bowl (MB) to poly(chloromethylstyrene-co-divinylbenzene) (PCD). By treatment of unreacted chloro groups of the resulting PCD with methoxide and destruction of the MB moieties attached to PCD with acid followed by addition of Cu(II) ion to the exposed tren moieties, catalytic polymers with peptidase activity were obtained. The average number (β) of proximal Cu(II)tren moieties in the active site of the artificial multinuclear metallopeptidase was determined by quantifying the Cu(II) content. Several species of the artificial metallopeptidases with different β contents were prepared and examined for catalytic activity in hydrolysis of various cinnamoyl amide derivatives. The PCD-based catalytic polymers did not hydrolyze a neutral amide but effectively hydrolyzed carboxyl-containing amides (N-cinnamoyl glycine, N-cinnamoyl β-alanine, and N-cinnamoyl γ-amino butyrate). Analysis of the kinetic data revealed that the active sites comprising three Cu(II)tren units were mainly responsible for the catalytic activity. When analyzed in terms of k(cat), the catalytic activity of the PCD-based artificial peptidase was comparable to or better than the catalytic antibody with the highest peptidase activity reported to date. A mechanism is suggested for the effective cooperation among the three metal centers of the active site in hydrolysis of the carboxyl-containing amides.
KINETICS OF THE FORMATION OF PANTOLACTONE FROM PANTOTHENATES AND ITS QUANTITATIVE DETERMINATION
Moiseenok, A. G.,Slyshenkov, V. S.,Lysenkova, A. V.
, p. 88 - 90 (1984)
The conditions of hydrolysis and lactonization of the calcium and sodium salts of pantothenic and pantoic acids have been studied.The selected conditions of hydrolysis (t = 80 deg C, CHCl = 13percent) led to a 100percent yield of β-alanine and pantothenates after 60 min from the beginning of hydrolysis, while the formation of pantolactone was complete in 105 min for the calcium salt and in 75 min for the sodium salt.The hydrolysis and lactonization reactions have been performed under the conditions mentioned, and the GLC of the pantolactone formed has permitted the determination of various concentrations of calcium pantothenate.The results obtained from the GLC analysis of pantolactone indicate the possibility of a quantitative determination of salts of pantothenic and pantoic acids.The sensitivity of this method is 0.2-5 nmole.
A green-by-design bioprocess for l-carnosine production integrating enzymatic synthesis with membrane separation
Yin, Dong-Ya,Pan, Jiang,Zhu, Jie,Liu, You-Yan,Xu, Jian-He
, p. 5971 - 5978 (2019)
l-Carnosine (l-Car, β-alanyl-l-histidine) is a bioactive dipeptide with important physiological functions. Direct coupling of unprotected β-Ala (β-alanine) with l-His (l-histidine) mediated by an enzyme is a promising method for l-Car synthesis. In this study, a new recombinant dipeptidase (SmPepD) from Serratia marcescens with a high synthetic activity toward l-Car was identified by a genome mining approach and successfully expressed in Escherichia coli. Divalent metal ions strongly promoted the synthetic activity of SmPepD, with up to 21.7-fold increase of activity in the presence of 0.1 mM MnCl2. Higher temperature, lower pH and increasing substrate loadings facilitated the l-Car synthesis. Pilot biocatalytic syntheses of l-Car were performed comparatively in batch and continuous modes. In the continuous process, an ultra-filtration membrane reactor with a working volume of 5 L was employed for catalyst retention. The dipeptidase, SmPepD, showed excellent operational stability without a significant decrease in space-time yield after 4 days. The specific yield of l-Car achieved was 105 gCar gcatalyst-1 by the continuous process and 30.1 gCar gcatalyst-1 by the batch process. A nanofiltration membrane was used to isolate the desired product l-Car from the reaction mixture by selectively removing the excess substrates, β-Ala and l-His. As a result, the final l-Car content was effectively enriched from 2.3% to above 95%, which gave l-Car in 99% purity after ethanol precipitation with a total yield of 60.2%. The recovered substrate mixture of β-Ala and l-His can be easily reused, which will enable the economically attractive and environmentally benign production of the dipeptide l-Car.
Fixation of Molecular Nitrogen Using Aliphatic Carboxylic Acid by Nitrogen Arc Plasma. Formation of Amino Acids
Takasaki, Michiaki,Harada, Kaoru
, p. 365 - 368 (1987)
When argon-nitrogen plasma was blown into an aqueous solution containing aliphatic carboxylic acids, formation of several amino acids and amines was identified.
TRANSFORMATIONS OF ACRYLAMIDE AND POLYACRYLAMIDE AT HIGH PRESSURES AND LARGE SHEAR DEFORMATIONS
Chistotina, N. P.,Zharov, A. A.
, p. 944 - 949 (1992)
Radical polymerization and nucleophilic addition of an amide group to the double bond of acrylamide take place parallel in conditions of shear deformation and high pressures (up to 8 GPa). Large shear deformations cause the formation of β-alanine as the result of reactions of hydrolysis of amide groups and peptide bonds. Keywords: pressure, shear deformation, acrylamide, polyacrylamide, radical polymerization, nucleophilic addition, hydrolysis, β-alanine.
Kinetic and spectroscopic evidence of negative cooperativity in the action of lysine 2,3-aminomutase
Ruzicka, Frank J.,Frey, Perry A.
, p. 16118 - 16124 (2010)
Lysine 2,3-aminomutase (LAM) catalyzes the interconversion of l-lysine and l-β-lysine, a component of a number of antibiotics. The reaction requires the cofactors S-adenosyl-l-methionine (SAM), pyridoxal-5′-phosphate (PLP), and a [4Fe-4S] cluster. LAM is a founding member of the radical SAM superfamily of enzymes. LAM is highly specific for l-lysine and will not accept most other amino acids as substrates. l-Alanine and l-2-aminobutyrate at 0.2 M react as substrates for LAM at, respectively, 5 × 10-6 and 8 × 10-5 times the rate with saturating l-lysine. Saturating ethylamine accelerates the l-alanine reaction 70-fold, and saturating methylamine accelerates the l-2-aminobutyrate reaction 47-fold. The primary amines binding at the active site of LAM with l-alanine or l-2-aminobutyrate simulate l-lysine. The steady-state kinetics of the reaction of l-alanine + ethylamine displays negative cooperativity with respect to l-alanine. The second-order rate constant for production of β-alanine in the reaction of l-alanine and saturating ethylamine is 0.040 M-1 s-1, which is 2 × 10 -5 times the value of kcat/Km for the reaction of l-lysine. When l-lysine is at a concentration 1/16th of Km, the lysyl-free radical intermediate is hardly detectable by EPR; however, the addition of l-alanine at high concentration (0.2 M) enhances free radical formation, and the addition of ethylamine further enhances radical formation. These facts complement the kinetic observations and support negative cooperativity in the reaction of l-alanine as a substrate for LAM. Present results and independent evidence support negative cooperativity in the reaction of l-lysine as well.
