Relevant bibliographies by topics / Bi-substrate enzymatic reactions

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Academic literature on the topic 'Bi-substrate enzymatic reactions'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Bi-substrate enzymatic reactions"

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Klaus, Tobias, Alexander Seifert, Tim Häbe, Bettina Nestl, and Bernhard Hauer. "An Enzyme Cascade Synthesis of Vanillin." Catalysts 9, no. 3 (2019): 252. http://dx.doi.org/10.3390/catal9030252.

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A novel approach for the synthesis of vanillin employing a three-step two-enzymatic cascade sequence is reported. Cytochrome P450 monooxygenases are known to catalyse the selective hydroxylation of aromatic compounds, which is one of the most challenging chemical reactions. A set of rationally designed variants of CYP102A1 (P450 BM3) from Bacillus megaterium at the amino acid positions 47, 51, 87, 328 and 437 was screened for conversion of the substrate 3-methylanisole to vanillyl alcohol via the intermediate product 4-methylguaiacol. Furthermore, a vanillyl alcohol oxidase (VAO) variant (F454
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Holderbaum, Daniel Ferreira, Tomoyuki Kon, Tsuyoshi Kudo, and Miguel Pedro Guerra. "Enzymatic Browning, Polyphenol Oxidase Activity, and Polyphenols in Four Apple Cultivars: Dynamics during Fruit Development." HortScience 45, no. 8 (2010): 1150–54. http://dx.doi.org/10.21273/hortsci.45.8.1150.

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Enzymatic browning is one of the most important reactions that occur in fruits and vegetables, usually resulting in negative effects on color, taste, flavor, and nutritional value. The reaction is a consequence of phenolic compounds' oxidation by polyphenol oxidase (PPO), which triggers the generation of dark pigments. This is particularly relevant for apples, which are rich in polyphenols and highly susceptible to enzymatic browning. The objective of the present work was to quantify enzymatic browning and PPO activity and identify and quantify target polyphenols in apple [Malus ×sylvestris (L
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Ichikawa, Konatsu, Taiki Adachi, Keisei Sowa, Yuki Kitazumi, and Osamu Shirai. "Bioelectrochemical Characterization of a Molybdenum-Containing Aldehyde Dehydrogenase Variant Deleting Its Cytochrome C Subunit." ECS Meeting Abstracts MA2024-02, no. 67 (2024): 4722. https://doi.org/10.1149/ma2024-02674722mtgabs.

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Bioelectrocatalysis is a coupled system with enzymatic and electrode reactions. Some oxidoreductases can directly communicate with electrodes, which is called direct electron transfer (direct ET; DET)-type bioelectrocatalysis. The number of enzymes proceeding with DET-type reactions is still limited, and its mechanism is not fully elucidated. However, it is expected to be applied to electrochemical devices such as biosensors, biofuel cells, and bioreactors, owing to energy efficiency, biocompatibility, and design flexibility. In addition, this reaction is utilized for enzyme characterization b
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Wang, Zhi-Xin, and Jia-Wei Wu. "The Complete Pathway for ERK2-catalyzed Reaction." Journal of Biological Chemistry 282, no. 38 (2007): 27678–84. http://dx.doi.org/10.1074/jbc.m703161200.

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In the present study, the enzymatic mechanism of ERK2 is re-examined by a combination of steady-state kinetic studies in the absence and presence of viscosogenic agents. Kinetic studies carried out in various concentrations of sucrose revealed that both kcat and kcat/Km for either ATP or EtsΔ138 were highlysensitive to solvent viscosity, suggesting that the rapid equilibrium assumption is not valid for the phosphorylation of protein substrate by ERK2. Furthermore, the kinetic analysis with the minimal random Bi Bi reaction mechanism is shown to be inconsistent with the principle of the detaile
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Gawas, Sarita D., Nidya Lokanath, and Virendra K. Rathod. "Optimization of enzymatic synthesis of ethyl hexanoate in a solvent free system using response surface methodology (RSM)." Biocatalysis 4, no. 1 (2018): 14–26. http://dx.doi.org/10.1515/boca-2018-0002.

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Abstract The present paper demonstrates application of biocatalysis to the synthesis of ethyl hexanoate, i.e. pineapple flavour ester, in a solvent free system. In order to evaluate the effect of various process parameters on reaction conversion, response surface methodology (RSM) complemented by central composite design (CCD) was employed. A maximum conversion of 88.57% was obtained while changing one factor at a time, at optimum conditions of temperature (50 °C), enzyme dose (2%), molar ratio acid to alcohol (1:3), speed of agitation 250 rpm and reaction time of 120 min. Based on this RSM st
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Tamborini, Lucia, Clelia Previtali, Francesca Annunziata, et al. "An Enzymatic Flow-Based Preparative Route to Vidarabine." Molecules 25, no. 5 (2020): 1223. http://dx.doi.org/10.3390/molecules25051223.

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The bi-enzymatic synthesis of the antiviral drug vidarabine (arabinosyladenine, ara-A), catalyzed by uridine phosphorylase from Clostridium perfringens (CpUP) and a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP), was re-designed under continuous-flow conditions. Glyoxyl–agarose and EziGTM1 (Opal) were used as immobilization carriers for carrying out this preparative biotransformation. Upon setting-up reaction parameters (substrate concentration and molar ratio, temperature, pressure, residence time), 1 g of vidarabine was obtained in 55% isolated yield and >99% purity by
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7

Mizanur, Rahman M., Amanda K. K. Griffin та Nicola L. Pohl. "Recombinant production and biochemical characterization of a hyperthermostable α-glucan/maltodextrin phosphorylase fromPyrococcus furiosus". Archaea 2, № 3 (2008): 169–76. http://dx.doi.org/10.1155/2008/549759.

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Alpha-glucan phosphorylase catalyzes the reversible cleavage of α-1-4-linked glucose polymers into α-D-glucose-1-phosphate. We report the recombinant production of an α-glucan/maltodextrin phosphorylase (PF1535) from a hyperthermophilic archaeon,Pyrococcus furiosus, and the first detailed biochemical characterization of this enzyme from any archaeal source using a mass-spectrometry-based assay. The apparent 98 kDa recombinant enzyme was active over a broad range of temperatures and pH, with optimal activity at 80 °C and pH 6.5–7. This archaeal protein retained its complete activity after 24 h
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8

Weiss, Alexander K. H., Andreas Naschberger, Johannes R. Loeffler, et al. "Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1." Biochemical Journal 475, no. 22 (2018): 3561–76. http://dx.doi.org/10.1042/bcj20180750.

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Whereas enzymes in the fumarylacetoacetate hydrolase (FAH) superfamily catalyze several distinct chemical reactions, the structural basis for their multi-functionality remains elusive. As a well-studied example, human FAH domain-containing protein 1 (FAHD1) is a mitochondrial protein displaying both acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. As mitochondrial ODx, FAHD1 acts antagonistically to pyruvate carboxylase, a key metabolic enzyme. Despite its importance for mitochondrial function, very little is known about the catalytic mechanisms underlying FAHD1 enzy
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Lee, Jung-Kul, Bong-Seong Koo, Sang-Yong Kim, and Hyung-Hwan Hyun. "Purification and Characterization of a Novel Mannitol Dehydrogenase from a Newly Isolated Strain of Candida magnoliae." Applied and Environmental Microbiology 69, no. 8 (2003): 4438–47. http://dx.doi.org/10.1128/aem.69.8.4438-4447.2003.

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ABSTRACT Mannitol biosynthesis in Candida magnoliae HH-01 (KCCM-10252), a yeast strain that is currently used for the industrial production of mannitol, is catalyzed by mannitol dehydrogenase (MDH) (EC 1.1.1.138). In this study, NAD(P)H-dependent MDH was purified to homogeneity from C. magnoliae HH-01 by ion-exchange chromatography, hydrophobic interaction chromatography, and affinity chromatography. The relative molecular masses of C. magnoliae MDH, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and size-exclusion chromatography, were 35 and 142 kDa, respectively,
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Demkiv, Olha, Galina Gayda, Nataliya Stasyuk, Olena Brahinetz, Mykhailo Gonchar, and Marina Nisnevitch. "Nanomaterials as Redox Mediators in Laccase-Based Amperometric Biosensors for Catechol Assay." Biosensors 12, no. 9 (2022): 741. http://dx.doi.org/10.3390/bios12090741.

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Laccase is a copper-containing enzyme that does not require hydrogen peroxide as a co-substrate or additional cofactors for an enzymatic reaction. Nanomaterials of various chemical structures are usually applied to the construction of enzyme-based biosensors. Metals, metal oxides, semiconductors, and composite NPs perform various functions in electrochemical transformation schemes as a platform for the enzyme immobilization, a mediator of an electron transfer, and a signal amplifier. We describe here the development of amperometric biosensors (ABSs) based on laccase and redox-active micro/nano
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Conference papers on the topic "Bi-substrate enzymatic reactions"

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MAGARIO, Ivana, José SCILIPOTI, and Salvador Eduardo BRANDOLÍN. "ACTIVITY-BASED KINETIC MODELLING OF LIPASE CATALYSED SYNTHESIS OF PEROCTANOIC ACID." In SOUTHERN BRAZILIAN JOURNAL OF CHEMISTRY 2021 INTERNATIONAL VIRTUAL CONFERENCE. DR. D. SCIENTIFIC CONSULTING, 2022. http://dx.doi.org/10.48141/sbjchem.21scon.12_abstract_brandolin.pdf.

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Carboxylic peroxy acids are organic oxidants of relevance in the cosmetic, food, and agrochemical industries. However, they are traditionally used as intermediaries in a process known as Prileschajew epoxidation and synthesized using sulfuric acid as a catalyst, promoting undesirable reactions on the final epoxides. Therefore, the study of selective catalysts such as enzymes is a topic of interest. In this work, peroctanoic acid synthesis was carried out using n-hexane as the solvent and an immobilized Candida Antarctica Lipase B commercial preparation as the catalyst. On the other hand, the o
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