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

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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9

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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10

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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11

Dall'Antonia, Luiz Henrique, and Luan Pereira Camargo. "(Invited) Photoelectrochemical Properties of Binary Vanadate Oxides: A Comprehensive Synthesis/Application Relationship." ECS Meeting Abstracts MA2025-01, no. 56 (2025): 2725. https://doi.org/10.1149/ma2025-01562725mtgabs.

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The development of novel materials with catalytic and energy storage properties is essential due to increasing industrial growth, energy crises, environmental challenges, and rising global energy demands. Binary metal oxides outperform single-component oxides, offering higher electrical conductivity, versatile oxidation states, and tunable structures. Among these, vanadate-based materials (MxVyOz, where M = Bi, Fe, Cu, Ce) have gained attention for their low band gap energy (visible light absorption), excellent chemical and thermal stability, low toxicity, high elemental abundance, and synergi

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12

Rafayel, A. Azizyan, E. Gevorgyan Aram, B. Arakelyan Valeri, and S. Gevorgyan Emil. "Mathematical Modeling of Uncompetitive Inhibition of Bi-Substrate Enzymatic Reactions." September 6, 2013. https://doi.org/10.5281/zenodo.1088248.

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Currently, mathematical and computer modeling are widely used in different biological studies to predict or assess behavior of such a complex systems as a biological are. This study deals with mathematical and computer modeling of bi-substrate enzymatic reactions, which play an important role in different biochemical pathways. The main objective of this study is to represent the results from <i>in silico</i> investigation of bi-substrate enzymatic reactions in the presence of uncompetitive inhibitors, as well as to describe in details the inhibition effects. Four models of uncompetitive inhibi

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13

Rafayel, A. Azizyan, E. Gevogyan Aram, B. Arakelyan Valeri, and S. Gevorgyan Emil. "Mathematical modeling of Bi-Substrate Enzymatic Reactions with Ping-Pong Mechanism in the Presence of Competitive Inhibitors." February 27, 2013. https://doi.org/10.5281/zenodo.1073187.

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The mathematical modeling of different biological processes is usually used to predict or assess behavior of systems in which these processes take place. This study deals with mathematical and computer modeling of bi-substrate enzymatic reactions with ping-pong mechanism, which play an important role in different biochemical pathways. Besides that, three models of competitive inhibition were designed using different software packages. The main objective of this study is to represent the results from in silico investigation of bi-substrate enzymatic reactions with ordered pingpong mechanism in

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14

Zhang, Xin, Jiyu Xin, Zhiguo Wang, et al. "Structural basis of a bi-functional malonyl-CoA reductase (MCR) from the photosynthetic green non-sulfur bacterium Roseiflexus castenholzii." mBio, June 6, 2023. http://dx.doi.org/10.1128/mbio.03233-22.

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ABSTRACT Malonyl-CoA reductase (MCR) is a NADPH-dependent bi-functional enzyme that performs alcohol dehydrogenase and aldehyde dehydrogenase (CoA-acylating) activities in the N- and C-terminal fragments, respectively. It catalyzes the two-step reduction of malonyl-CoA to 3-hydroxypropionate (3-HP), a key reaction in the autotrophic CO 2 fixation cycles of Chloroflexaceae green non-sulfur bacteria and the archaea Crenarchaeota . However, the structural basis underlying substrate selection, coordination, and the subsequent catalytic reactions of full-length MCR is largely unknown. For the first

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15

Turner, Madison, Olivier Tremblay, Kayla A. Heney, et al. "Characterization of C3larvinA, a novel RhoA-targeting ADP-ribosyltransferase toxin produced by the honey bee pathogen, Paenibacillus larvae." Bioscience Reports 40, no. 1 (2020). http://dx.doi.org/10.1042/bsr20193405.

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Abstract C3larvinA is a putative virulence factor produced by Paenibacillus larvae enterobacterial-repetitive-intergenic-consensus (ERIC) III/IV (strain 11-8051). Biochemical, functional and structural analyses of C3larvinA revealed that it belongs to the C3-like mono-ADP-ribosylating toxin subgroup. Mammalian RhoA was the target substrate for its transferase activity suggesting that it may be the biological target of C3larvinA. The kinetic parameters of the NAD+ substrate for the transferase (KM = 75 ± 10 µM) and glycohydrolase (GH) (KM = 107 ± 20 µM) reactions were typical for a C3-like bact

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16

Bai, Shaowei, Liangzhen Yang, Honglei Wang, et al. "Cellobiose phosphorylase from Caldicellulosiruptor bescii catalyzes reversible phosphorolysis via different kinetic mechanisms." Scientific Reports 12, no. 1 (2022). http://dx.doi.org/10.1038/s41598-022-08036-z.

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AbstractIn the process of yielding biofuels from cellulose degradation, traditional enzymatic hydrolysis, such as β-glucosidase catalyzing cellobiose, can barely resolve the contradiction between cellulose degradation and bioenergy conservation. However, it has been shown that cellobiose phosphorylase provides energetic advantages for cellobiose degradation through a phosphorolytic pathway, which has attracted wide attention. Here, the cellobiose phosphorylase gene from Caldicellulosiruptor bescii (CbCBP) was cloned, expressed, and purified. Analysis of the enzymatic properties and kinetic mec

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17

Mahdi, Wael A., Mohammad S. Absar, Suna Choi, Victor C. Yang, and Young M. Kwon. "Enhanced control of bioactivity of tissue plasminogen activator (tPA) through domain-directed enzymatic oxidation of terminal galactose." BioImpacts, October 31, 2022. http://dx.doi.org/10.34172/bi.2022.23477.

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Introduction: In targeted enzyme prodrug constructs, it is critical to control the bioactivity of the drug in its prodrug form. The preparation of such constructs often involves conjugation reactions directed to functional groups on amino acid side chains of the protein, which result in random conjugation and incomplete control of bioactivity of a prodrug, which may result in significant nontarget effect. Thus, more specific method of modification is desired. If the drug is a glycoprotein, enzymatic oxidation may offer an alternative approach for therapeutic glycoproteins. Methods: Tissue plas

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18

Yadav, Ganapati D., and Somnath Dattatray Shinde. "Kinetic Modeling and Optimization of Immobilized Candida antarctica Lipase B Catalysed Synthesis of Butyl-4-Methyl-3-Oxopentanoate using Response Surface Methodology." International Journal of Chemical Reactor Engineering 10, no. 1 (2012). http://dx.doi.org/10.1515/1542-6580.2981.

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Abstract Response surface methodology (RSM) was used to model and optimize the immobilized Candida antarctica lipase B catalysed synthesis of butyl-4-methyl-3-oxopentanoate. To determine optimum conditions of the transesterification, a four-factor and five-level central composite rotatable design (CCRD) was used. The factors studied were enzyme load (A), reaction temperature (B), methyl-4-methyl-3-oxopentanoate concentration (C) and n-butanol concentration (D). A quadratic polynomial regression model was used to analyze the experimental data at a 95% confidence level (p < 0.05). The results

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19

Saburi, Wataru, Takanori Nihira, Hiroyuki Nakai, Motomitsu Kitaoka, and Haruhide Mori. "Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose." Scientific Reports 12, no. 1 (2022). http://dx.doi.org/10.1038/s41598-021-04421-2.

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AbstractGlycoside phosphorylases (GPs), which catalyze the reversible phosphorolysis of glycosides, are promising enzymes for the efficient production of glycosides. Various GPs with new catalytic activities are discovered from uncharacterized proteins phylogenetically distant from known enzymes in the past decade. In this study, we characterized Paenibacillus borealis PBOR_28850 protein, belonging to glycoside hydrolase family 94. Screening of acceptor substrates for reverse phosphorolysis, in which α-d-glucose 1-phosphate was used as the donor substrate, revealed that the recombinant PBOR_28

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20

Shariatzadeh, Siavash, Sepehr Shafiee, Ali Zafari, et al. "Developing a pro-angiogenic placenta derived amniochorionic scaffold with two exposed basement membranes as substrates for cultivating endothelial cells." Scientific Reports 11, no. 1 (2021). http://dx.doi.org/10.1038/s41598-021-01922-y.

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AbstractDecellularized and de-epithelialized placenta membranes have widely been used as scaffolds and grafts in tissue engineering and regenerative medicine. Exceptional pro-angiogenic and biomechanical properties and low immunogenicity have made the amniochorionic membrane a unique substrate which provides an enriched niche for cellular growth. Herein, an optimized combination of enzymatic solutions (based on streptokinase) with mechanical scrapping is used to remove the amniotic epithelium and chorion trophoblastic layer, which resulted in exposing the basement membranes of both sides witho

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21

Chen, Hefeng, Ran Liu, Shengliang Cai та ін. "Intermediate product control in cascade reaction for one‐pot production of ε‐caprolactone by Escherichia coli". Biotechnology Journal 19, № 2 (2024). http://dx.doi.org/10.1002/biot.202300210.

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Abstractε‐Caprolactone is an important non‐toxic compound for polymer synthesis like polycaprolactone which has been widely used in drug delivery and degradable plastics. To meet the demand for a green economy, a bi‐enzymatic cascade, consisting of an alcohol dehydrogenase (ADH) and a cyclohexanone monooxygenase (CHMO), was designed and introduced into Escherichia coli to synthesize ε‐caprolactone from cyclohexanol with a self‐sufficient NADPH‐cofactor regeneration system. To further improve the catalytic efficiency, a carbonyl group‐dependent colorimetric method using inexpensive 2,4‐dinitrop

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