Relevant bibliographies by topics / Phenylglyoxal conversion

Academic literature on the topic 'Phenylglyoxal conversion'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Phenylglyoxal conversion"

1

Xu, Haimei, Zichun Wang, Zhichao Miao, Yuxiang Zhu, Aleksei Marianov, Lizhuo Wang, Patrice Castignolles, Marianne Gaborieau, Jun Huang, and Yijiao Jiang. "Correlation between Acidity and Catalytic Performance of Mesoporous Zirconium Oxophosphate in Phenylglyoxal Conversion." ACS Sustainable Chemistry & Engineering 7, no. 9 (March 31, 2019): 8931–42. http://dx.doi.org/10.1021/acssuschemeng.9b00989.

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2

Wang, Zichun, Yijiao Jiang, Alfons Baiker, and Jun Huang. "Efficient Acid-Catalyzed Conversion of Phenylglyoxal to Mandelates on Flame-Derived Silica/Alumina." ACS Catalysis 3, no. 7 (June 14, 2013): 1573–77. http://dx.doi.org/10.1021/cs400271e.

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3

Wang, Zichun, Yijiao Jiang, Michael Hunger, Alfons Baiker, and Jun Huang. "Catalytic Performance of Brønsted and Lewis Acid Sites in Phenylglyoxal Conversion on Flame-Derived Silica-Zirconia." ChemCatChem 6, no. 10 (September 1, 2014): 2970–75. http://dx.doi.org/10.1002/cctc.201402397.

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4

Misra, K., A. B. Banerjee, S. Ray, and M. Ray. "Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into d-lactate without reduced glutathione." Biochemical Journal 305, no. 3 (February 1, 1995): 999–1003. http://dx.doi.org/10.1042/bj3050999.

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A single novel enzyme, glyoxalase III, which catalyses the conversion of methylglyoxal into D-lactate without involvement of GSH, has been detected in and purified from Escherichia coli. Of several carbonyl compounds tested, only the alpha-ketoaldehydes methylglyoxal and phenylglyoxal were found to be substrates for this enzyme. Glyoxalase III is active over a wide range of pH with no sharp pH optimum. In its native form it has an M(r) of 82000 +/- 2000, and it is composed of two subunits of equal M(r). Glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III. Glyoxalase III is found to be sensitive to thiol-blocking reagents. The p-hydroxymercuribenzoate-inactivated enzyme could be almost completely re-activated by dithiothreitol and other thiol-group-containing compounds, indicating the possible involvement of thiol group(s) at or near the active site of the enzyme.
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5

Wang, Zichun, Yijiao Jiang, Rafal Rachwalik, Zhongwen Liu, Jeffrey Shi, Michael Hunger, and Jun Huang. "One-Step Room-Temperature Synthesis of [Al]MCM-41 Materials for the Catalytic Conversion of Phenylglyoxal to Ethylmandelate." ChemCatChem 5, no. 12 (September 9, 2013): 3889–96. http://dx.doi.org/10.1002/cctc.201300375.

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6

Hoover, Gordon J., Owen R. Van Cauwenberghe, Kevin E. Breitkreuz, Shawn M. Clark, A. Rod Merrill, and Barry J. Shelp. "Characteristics of an Arabidopsis glyoxylate reductase: general biochemical properties and substrate specificity for the recombinant protein, and developmental expression and implications for glyoxylate and succinic semialdehyde metabolism in planta." Canadian Journal of Botany 85, no. 9 (September 2007): 883–95. http://dx.doi.org/10.1139/b07-081.

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Constitutive expression of an Arabidopsis thaliana (L.) Heynh cDNA (GenBank accession No. AY044183 ) in a succinic semialdehyde (SSA) dehydrogenase-deficient yeast ( Saccharomyces cerevisiae Hansen) mutant enables growth on γ-aminobutyrate and significantly enhances the accumulation of γ-hydroxybutyrate. In this report, the cDNA (designated hereinafter as AtGR1) was functionally expressed in Escherichia coli , and the recombinant protein purified to homogeneity. Kinetic analysis of substrate specificity revealed that the enzyme catalyzed the conversion of glyoxylate to glycolate (Km, glyoxylate = 4.5 μmol·L–1) as well as SSA to γ-hydroxybutyrate (Km, SSA = 0.87 mmol·L–1) via an essentially irreversible, NADPH-based mechanism. The enzyme had a 250-fold higher preference for glyoxylate than SSA based on the performance constants (kcat/Km), and with the exception of 4-carboxybenzaldehyde, at least a 100-fold higher preference for SSA than all other substrates tested (formaldehyde, acetaldehyde, butyraldehyde, 2-carboxybenzaldehyde, glyoxal, methylglyoxal, phenylglyoxal, phenylglyoxylate). In vitro assays of SSA reductase activity in cell-free extracts from Arabidopisis revealed its presence throughout the plant, although its specific activity was considerably higher in leaves at all developmental stages and in reproductive parts than in roots. It is proposed that the enzyme functions in redox homeostasis and the detoxification of both glyoxylate and SSA, in planta, resulting in the production of glycolate and γ-hydroxybutyrate, respectively.
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7

Zhang, S., J. D. McCarter, Y. Okamura-Oho, F. Yaghi, A. Hinek, S. G. Withers, and J. W. Callahan. "Kinetic mechanism and characterization of human β-galactosidase precursor secreted by permanently transfected Chinese hamster ovary cells." Biochemical Journal 304, no. 1 (November 15, 1994): 281–88. http://dx.doi.org/10.1042/bj3040281.

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Chinese hamster ovary cell clones permanently transfected with the cDNA for human lysosomal beta-galactosidase secrete the enzyme precursor into the cell medium, from which it is purified to apparent homogeneity in a single step by affinity chromatography. The purified precursor is fully active, displays the same pH optimum and Km values as the mature placental enzyme, and has an intact C-terminus. The intact enzyme when chromatographed on a Sephacryl S-200 molecular-sieve column elutes as a 105,500 Da monomer, whereas on SDS/PAGE gels the polypeptide migrates as an 88 kDa polypeptide. A time course of digestion with glycopeptide-N-glycanase shows the gradual conversion of the precursor from an 88 to a 72 kDa protein, suggesting the presence of five N-linked oligosaccharides in the protein. The precursor is readily taken up in a mannose-6-phosphate-dependent manner into beta-galactosidase-deficient, GM1-gangliosidosis fibroblasts, and the enzyme activity is returned to normal levels. We show that the stereochemical course of enzymic hydrolysis involves the retention of the beta-configuration at the anomeric centre, suggesting a double-displacement mechanism. Furthermore, the enzyme is rapidly and irreversibly inactivated in the presence of the mechanism-based inactivator 2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-galactopyranoside, which implicates a covalent intermediate. The enzyme is also inactivated by 1-ethyl-3(3-dimethylamino-propyl)carbodi-imide and by phenylglyoxal, which implicates carboxylate and arginine residues respectively in the active site. We conclude that the beta-galactosidase precursor is functionally identical to the mature lysosomal form of the enzyme and serves as an excellent enzyme source for investigation of structure-function relationships in the protein.
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8

Yang, Wenjie, Kyung Duk Kim, Luke A. O'Dell, Lizhuo Wang, Haimei Xu, Mengtong Ruan, Wei Wang, Ryong Ryoo, Yijiao Jiang, and Jun Huang. "Brønsted acid sites formation through penta-coordinated aluminum species on alumina-boria for phenylglyoxal conversion." Journal of Catalysis, November 2022. http://dx.doi.org/10.1016/j.jcat.2022.11.012.

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