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Journal articles on the topic 'Tailoring enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Moin, Syed, and Muhammad Omar. "Laccase Enzymes: Purification, Structure to Catalysis and Tailoring." Protein & Peptide Letters 21, no. 8 (2013): 707–13. http://dx.doi.org/10.2174/09298665113209990058.

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2

Napan, Kandy, Shuwei Zhang, Whitney Morgan, Thomas Anderson, Jon Y. Takemoto, and Jixun Zhan. "Synergistic Actions of Tailoring Enzymes in Pradimicin Biosynthesis." ChemBioChem 15, no. 15 (2014): 2289–96. http://dx.doi.org/10.1002/cbic.201402306.

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3

Borgman, Paul, Ryan D. Lopez, and Amy L. Lane. "The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases." Organic & Biomolecular Chemistry 17, no. 9 (2019): 2305–14. http://dx.doi.org/10.1039/c8ob03063d.

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4

Gober, Redding, Ryan Wheeler, and Jürgen Rohr. "Post-PKS enzyme complexes." MedChemComm 10, no. 11 (2019): 1855–66. http://dx.doi.org/10.1039/c9md00066f.

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5

Mattiasson, B. "Tailoring the microenvironment of enzymes in water-poor systems." Trends in Biotechnology 9, no. 1 (1991): 394–98. http://dx.doi.org/10.1016/0167-7799(91)90132-2.

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6

Komor, Anna J., Andrew J. Jasniewski, Lawrence Que, and John D. Lipscomb. "Diiron monooxygenases in natural product biosynthesis." Natural Product Reports 35, no. 7 (2018): 646–59. http://dx.doi.org/10.1039/c7np00061h.

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7

Kim, Ki-Bong, and Kie-Jung Park. "Computational Approach for Biosynthetic Engineering of Post-PKS Tailoring Enzymes." Genomics & Informatics 6, no. 4 (2008): 227–30. http://dx.doi.org/10.5808/gi.2008.6.4.227.

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8

Gabriel, Doris, Marino A. Campo, Robert Gurny, and Norbert Lange. "Tailoring Protease-Sensitive Photodynamic Agents to Specific Disease-Associated Enzymes." Bioconjugate Chemistry 18, no. 4 (2007): 1070–77. http://dx.doi.org/10.1021/bc060321l.

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9

Jones, J. Bryan, and Grace DeSantis. "Toward Understanding and Tailoring the Specificity of Synthetically Useful Enzymes." Accounts of Chemical Research 32, no. 2 (1999): 99–107. http://dx.doi.org/10.1021/ar960078d.

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10

Weiss, Renate, Georg M. Guebitz, Alessandro Pellis, and Gibson S. Nyanhongo. "Harnessing the Power of Enzymes for Tailoring and Valorizing Lignin." Trends in Biotechnology 38, no. 11 (2020): 1215–31. http://dx.doi.org/10.1016/j.tibtech.2020.03.010.

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11

Cavallari, Larisa H. "Tailoring Drug Therapy Based on Genotype." Journal of Pharmacy Practice 25, no. 4 (2012): 413–16. http://dx.doi.org/10.1177/0897190012448311.

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Polymorphisms in genes encoding drug metabolizing enzymes, drug transporters, and drug targets can influence drug effects and contribute to inter-individual differences in drug response. Genotype for drug metabolizing enzymes and drug transporters can influence drug disposition in the body (pharmacokinetics), whereas genotype for drug targets may influence sensitivity to a drug (pharmacodynamics). In some cases, response to a particular drug is contingent on genotype for both drug disposition and drug target proteins. For example, warfarin dose requirements are influenced by both cytochrome P4

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12

Ebrahimi, Aida. "(Invited) Tailoring 2D Materials As Artificial Enzymes for Developing Electrochemical Biosensors." ECS Meeting Abstracts MA2021-01, no. 55 (2021): 1409. http://dx.doi.org/10.1149/ma2021-01551409mtgabs.

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13

Hubert, Catherine B., and Sarah M. Barry. "New chemistry from natural product biosynthesis." Biochemical Society Transactions 44, no. 3 (2016): 738–44. http://dx.doi.org/10.1042/bst20160063.

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Catalysts are a vital part of synthetic chemistry. However, there are still many important reactions for which catalysts have not been developed. The use of enzymes as biocatalysts for synthetic chemistry is growing in importance due to the drive towards sustainable methods for producing both bulk chemicals and high value compounds such as pharmaceuticals, and due to the ability of enzymes to catalyse chemical reactions with excellent stereoselectivity and regioselectivity. Such challenging transformations are a common feature of natural product biosynthetic pathways. In this mini-review, we d

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14

van Dijk, Johannes W. A., and Clay C. C. Wang. "Expanding the Chemical Space of Nonribosomal Peptide Synthetase-like Enzymes by Domain and Tailoring Enzyme Recombination." Organic Letters 20, no. 17 (2018): 5082–85. http://dx.doi.org/10.1021/acs.orglett.8b01581.

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15

Winn, M., J. K. Fyans, Y. Zhuo, and J. Micklefield. "Recent advances in engineering nonribosomal peptide assembly lines." Natural Product Reports 33, no. 2 (2016): 317–47. http://dx.doi.org/10.1039/c5np00099h.

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This reviews summarises progress towards the engineering of nonribosomal peptide synthetases (NRPS) from the expression of heterologous tailoring enzymes to direct modifications of the assembly lines to produce analogues. New techniques/tools for introducing changes are also examined.

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16

He, Yi, and Russell J. Cox. "The molecular steps of citrinin biosynthesis in fungi." Chemical Science 7, no. 3 (2016): 2119–27. http://dx.doi.org/10.1039/c5sc04027b.

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Heterologous expression of the citrinin polyketide synthase, CitS, plus the tailoring enzymes CitA–CitE fromMonascus ruberhas fully elucidated the biosynthetic pathway to citrinin for the first time, showing relationships to tropolone, azaphilone and sorbicillinoid biosynthetic pathways in fungi.

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17

Jones, J. Bryan, and Grace Desantis. "ChemInform Abstract: Toward Understanding and Tailoring the Specificity of Synthetically Useful Enzymes." ChemInform 30, no. 18 (2010): no. http://dx.doi.org/10.1002/chin.199918314.

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18

Banik, Jacob J., Jeffrey W. Craig, Paula Y. Calle, and Sean F. Brady. "Tailoring Enzyme-Rich Environmental DNA Clones: A Source of Enzymes for Generating Libraries of Unnatural Natural Products." Journal of the American Chemical Society 132, no. 44 (2010): 15661–70. http://dx.doi.org/10.1021/ja105825a.

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19

Nguyen, Hoang-Chuong, Emmanuelle Darbon, Robert Thai, Jean-Luc Pernodet, and Sylvie Lautru. "Post-PKS Tailoring Steps of the Spiramycin Macrolactone Ring in Streptomyces ambofaciens." Antimicrobial Agents and Chemotherapy 57, no. 8 (2013): 3836–42. http://dx.doi.org/10.1128/aac.00512-13.

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ABSTRACTSpiramycins are clinically important 16-member macrolide antibiotics produced byStreptomyces ambofaciens. Biosynthetic studies have established that the earliest lactonic intermediate in spiramycin biosynthesis, the macrolactone platenolide I, is synthesized by a type I modular polyketide synthase (PKS). Platenolide I then undergoes a series of post-PKS tailoring reactions yielding the final products, spiramycins I, II, and III. We recently characterized the post-PKS glycosylation steps of spiramycin biosynthesis inS. ambofaciens. We showed that three glycosyltransferases, Srm5, Srm29,

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20

Grünewald, Jan, and Mohamed A. Marahiel. "Chemoenzymatic and Template-Directed Synthesis of Bioactive Macrocyclic Peptides." Microbiology and Molecular Biology Reviews 70, no. 1 (2006): 121–46. http://dx.doi.org/10.1128/mmbr.70.1.121-146.2006.

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SUMMARY Non-ribosomally synthesized peptides have compelling biological activities ranging from antimicrobial to immunosuppressive and from cytostatic to antitumor. The broad spectrum of applications in modern medicine is reflected in the great structural diversity of these natural products. They contain unique building blocks, such as d-amino acids, fatty acids, sugar moieties, and heterocyclic elements, as well as halogenated, methylated, and formylated residues. In the past decades, significant progress has been made toward the understanding of the biosynthesis of these secondary metabolite

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21

Harken, Lauritz, and Shu-Ming Li. "Modifications of diketopiperazines assembled by cyclodipeptide synthases with cytochrome P450 enzymes." Applied Microbiology and Biotechnology 105, no. 6 (2021): 2277–85. http://dx.doi.org/10.1007/s00253-021-11178-1.

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Abstract2,5-Diketopiperazines are the smallest cyclic peptides comprising two amino acids connected via two peptide bonds. They can be biosynthesized in nature by two different enzyme families, either by nonribosomal peptide synthetases or by cyclodipeptide synthases. Due to the stable scaffold of the diketopiperazine ring, they can serve as precursors for further modifications by different tailoring enzymes, such as methyltransferases, prenyltransferases, oxidoreductases like cyclodipeptide oxidases, 2-oxoglutarate-dependent monooxygenases and cytochrome P450 enzymes, leading to the formation

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22

Do, Truc, Julia E. Page, and Suzanne Walker. "Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes." Journal of Biological Chemistry 295, no. 10 (2020): 3347–61. http://dx.doi.org/10.1074/jbc.rev119.010155.

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Bacteria account for 1000-fold more biomass than humans. They vary widely in shape and size. The morphological diversity of bacteria is due largely to the different peptidoglycan-based cell wall structures that encase bacterial cells. Although the basic structure of peptidoglycan is highly conserved, consisting of long glycan strands that are cross-linked by short peptide chains, the mature cell wall is chemically diverse. Peptidoglycan hydrolases and cell wall–tailoring enzymes that regulate glycan strand length, the degree of cross-linking, and the addition of other modifications to peptidog

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23

Patrikainen, Pekka, Pauli Kallio, Keqiang Fan, et al. "Tailoring Enzymes Involved in the Biosynthesis of Angucyclines Contain Latent Context-Dependent Catalytic Activities." Chemistry & Biology 19, no. 5 (2012): 647–55. http://dx.doi.org/10.1016/j.chembiol.2012.04.010.

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24

Ribeiro, Lucas Ferreira, Vanesa Amarelle, Luana de Fátima Alves, et al. "Genetically Engineered Proteins to Improve Biomass Conversion: New Advances and Challenges for Tailoring Biocatalysts." Molecules 24, no. 16 (2019): 2879. http://dx.doi.org/10.3390/molecules24162879.

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Protein engineering emerged as a powerful approach to generate more robust and efficient biocatalysts for bio-based economy applications, an alternative to ecologically toxic chemistries that rely on petroleum. On the quest for environmentally friendly technologies, sustainable and low-cost resources such as lignocellulosic plant-derived biomass are being used for the production of biofuels and fine chemicals. Since most of the enzymes used in the biorefinery industry act in suboptimal conditions, modification of their catalytic properties through protein rational design and in vitro evolution

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25

Zhang, Guojian, Yi Li, Lei Fang, and Blaine A. Pfeifer. "Tailoring pathway modularity in the biosynthesis of erythromycin analogs heterologously engineered in E. coli." Science Advances 1, no. 4 (2015): e1500077. http://dx.doi.org/10.1126/sciadv.1500077.

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Type I modular polyketide synthases are responsible for potent therapeutic compounds that include avermectin (antihelinthic), rapamycin (immunosuppressant), pikromycin (antibiotic), and erythromycin (antibiotic). However, compound access and biosynthetic manipulation are often complicated by properties of native production organisms, prompting an approach (termed heterologous biosynthesis) illustrated in this study through the reconstitution of the erythromycin pathway through Escherichia coli. Using this heterologous system, 16 tailoring pathways were introduced, systematically producing eigh

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26

Reimer, Janice M., Martin N. Aloise, Harold R. Powell, and T. Martin Schmeing. "Manipulation of an existing crystal form unexpectedly results in interwoven packing networks with pseudo-translational symmetry." Acta Crystallographica Section D Structural Biology 72, no. 10 (2016): 1130–36. http://dx.doi.org/10.1107/s2059798316013504.

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Nonribosomal peptide synthetases (NRPSs) are multimodular enzymes that synthesize a myriad of diverse molecules. Tailoring domains have been co-opted into NRPSs to introduce further variety into nonribosomal peptide products. Linear gramicidin synthetase contains a unique formylation-tailoring domain in its initiation module (F-A-PCP). The structure of the F-A di-domain has previously been determined in a crystal form which had large solvent channels and no density for the minor Asub subdomain. An attempt was made to take advantage of this packing by removing the Asub subdomain from the constr

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27

Walsh, Christopher T., Huawei Chen, Thomas A. Keating, et al. "Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines." Current Opinion in Chemical Biology 5, no. 5 (2001): 525–34. http://dx.doi.org/10.1016/s1367-5931(00)00235-0.

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28

Sun, Lei, Siyuan Wang, Shuwei Zhang, et al. "Characterization of Three Tailoring Enzymes in Dutomycin Biosynthesis and Generation of a Potent Antibacterial Analogue." ACS Chemical Biology 11, no. 7 (2016): 1992–2001. http://dx.doi.org/10.1021/acschembio.6b00245.

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29

Ma, Ming, Thomas Kwong, Si-Kyu Lim, Jianhua Ju, Jeremy R. Lohman, and Ben Shen. "Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity." Journal of the American Chemical Society 135, no. 7 (2013): 2489–92. http://dx.doi.org/10.1021/ja4002635.

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30

Aluko, Rotimi E. "Determination of Nutritional and Bioactive Properties of Peptides in Enzymatic Pea, Chickpea, and Mung Bean Protein Hydrolysates." Journal of AOAC INTERNATIONAL 91, no. 4 (2008): 947–56. http://dx.doi.org/10.1093/jaoac/91.4.947.

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Abstract Within the primary structure of many pea and mung bean proteins are peptide sequences that can potentially be used in the formulation of therapeutic products for the treatment and prevention of human diseases. However, these peptide sequences need protease treatments before they can be released free of the parent proteins. Unlike chemical hydrolysis, enzymatic treatment enables more efficient tailoring of peptide products without formation of toxic by-products or destruction of amino acids. This review provides information on current methods that have been used to convert inactive pea

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31

Tomalik-Scharte, Dorota, Dominique Maiter, Julia Kirchheiner, Hannah E. Ivison, Uwe Fuhr, and Wiebke Arlt. "Impaired hepatic drug and steroid metabolism in congenital adrenal hyperplasia due to P450 oxidoreductase deficiency." European Journal of Endocrinology 163, no. 6 (2010): 919–24. http://dx.doi.org/10.1530/eje-10-0764.

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ObjectivePatients with congenital adrenal hyperplasia due to P450 oxidoreductase (POR) deficiency (ORD) present with disordered sex development and glucocorticoid deficiency. This is due to disruption of electron transfer from mutant POR to microsomal cytochrome P450 (CYP) enzymes that play a key role in glucocorticoid and sex steroid synthesis. POR also transfers electrons to all major drug-metabolizing CYP enzymes, including CYP3A4 that inactivates glucocorticoid and oestrogens. However, whether ORD results in impairment of in vivo drug metabolism has never been studied.DesignWe studied an a

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32

Hammadi, Mohannad Saleh, Kui Cheng, and Wen Jian Weng. "Influence of Microstructure on Performance of TiO₂ Nanodots Film Based Biosensor Electrodes." Key Engineering Materials 605 (April 2014): 155–58. http://dx.doi.org/10.4028/www.scientific.net/kem.605.155.

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Electrochemical biosensors are widely applied in areas related to health monitors. Protein adsorptions on the electrode and direct electron transfer between enzymes and electrode have been recognized as key factors affecting sensor performance. In this work, TiO2nanodots films were prepared on Ti substrate to act as electrodes of biosensors. The effect of the nanodots film microstructure on electrode performance was carried out. It was found that the performances H2O2biosensor could be improved by tailoring TiO2nanodots film microstructure in the electrodes. The present work could provide an a

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33

Wu, Changsheng, Marnix H. Medema, Rianne M. Läkamp, et al. "Leucanicidin and Endophenasides Result from Methyl-Rhamnosylation by the Same Tailoring Enzymes in Kitasatospora sp. MBT66." ACS Chemical Biology 11, no. 2 (2015): 478–90. http://dx.doi.org/10.1021/acschembio.5b00801.

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34

Yim, Grace, Lindsay Kalan, Kalinka Koteva, et al. "Harnessing the Synthetic Capabilities of Glycopeptide Antibiotic Tailoring Enzymes: Characterization of the UK-68,597 Biosynthetic Cluster." ChemBioChem 15, no. 17 (2014): 2613–23. http://dx.doi.org/10.1002/cbic.201402179.

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35

Zhou, Shanshan, Lona M. Alkhalaf, Emmanuel LC de los Santos, and Gregory L. Challis. "Mechanistic insights into class B radical-S-adenosylmethionine methylases: ubiquitous tailoring enzymes in natural product biosynthesis." Current Opinion in Chemical Biology 35 (December 2016): 73–79. http://dx.doi.org/10.1016/j.cbpa.2016.08.021.

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36

Amir, Roey, Assaf Harnoy, Nitsan Papo, and Gadi Slor. "Mixing End Groups in Thiol-Ene/Yne Reactions as a Simple Approach toward Multienzyme-Responsive Polymeric Amphiphiles." Synlett 29, no. 19 (2018): 2582–87. http://dx.doi.org/10.1055/s-0037-1611340.

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Taking advantage of the high fidelity of thiol-ene and thiol-yne chemistries, we used mixtures of thiols to prepare degradable PEG-dendron amphiphiles functionalized with two different types of enzymatically cleavable end groups. By tuning the feed ratios of the two thiols, we achieved mixtures of hybrids with statistically different ratios of end groups. Studies of the disassembly of statistically mixed hybrids showed that these amphiphiles have higher degrees of response when incubated with each of the activating enzymes, whereas a greater degree of selectivity was observed for a control mix

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37

Gao, Yu, Anscha J. J. Zietsman, Melané A. Vivier, and John P. Moore. "Deconstructing Wine Grape Cell Walls with Enzymes During Winemaking: New Insights from Glycan Microarray Technology." Molecules 24, no. 1 (2019): 165. http://dx.doi.org/10.3390/molecules24010165.

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Enzyme-aid maceration is carried out in most modern winemaking industries with a range of positive impacts on wine production. However, inconsistencies in enzyme efficiency are an issue complicated by unclear targets (limited information available on berry cell wall architecture of different cultivars) and the complex wine environment (i.e., fermenting must). Recent studies have been performed to develop a clearer picture of grape cell wall structures, maceration effects, and interactions between important wine compounds and grape-derived polysaccharides. This review highlights critically impo

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38

Mitsuguchi, Hisashi, Yasuyo Seshime, Isao Fujii, Masaaki Shibuya, Yutaka Ebizuka, and Tetsuo Kushiro. "Biosynthesis of Steroidal Antibiotic Fusidanes: Functional Analysis of Oxidosqualene Cyclase and Subsequent Tailoring Enzymes from Aspergillus fumigatus." Journal of the American Chemical Society 131, no. 18 (2009): 6402–11. http://dx.doi.org/10.1021/ja8095976.

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39

Giansanti, Manuela, Terry Karimi, Isabella Faraoni, and Grazia Graziani. "High-Dose Vitamin C: Preclinical Evidence for Tailoring Treatment in Cancer Patients." Cancers 13, no. 6 (2021): 1428. http://dx.doi.org/10.3390/cancers13061428.

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High-dose vitamin C has been proposed as a potential therapeutic approach for patients with advanced tumors who failed previous treatment with chemotherapy. Due to vitamin C complex pharmacokinetics, only intravenous administration allows reaching sufficiently high plasma concentrations required for most of the antitumor effects observed in preclinical studies (>0.250 mM). Moreover, vitamin C entry into cells is tightly regulated by SVCT and GLUT transporters, and is cell type-dependent. Importantly, besides its well-recognized pro-oxidant effects, vitamin C modulates TET enzymes promoting

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40

Zhu, Qinghua, Qi Chen, Yongxiang Song, et al. "Deciphering the sugar biosynthetic pathway and tailoring steps of nucleoside antibiotic A201A unveils a GDP-l-galactose mutase." Proceedings of the National Academy of Sciences 114, no. 19 (2017): 4948–53. http://dx.doi.org/10.1073/pnas.1620191114.

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Galactose, a monosaccharide capable of assuming two possible configurational isomers (d-/l-), can exist as a six-membered ring, galactopyranose (Galp), or as a five-membered ring, galactofuranose (Galf). UDP-galactopyranose mutase (UGM) mediates the conversion of pyranose to furanose thereby providing a precursor for d-Galf. Moreover, UGM is critical to the virulence of numerous eukaryotic and prokaryotic human pathogens and thus represents an excellent antimicrobial drug target. However, the biosynthetic mechanism and relevant enzymes that drive l-Galf production have not yet been characteriz

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41

Pearson, Leanne A., Kevin D. Barrow, and Brett A. Neilan. "Characterization of the 2-Hydroxy-acid Dehydrogenase McyI, Encoded within the Microcystin Biosynthesis Gene Cluster of Microcystis aeruginosa PCC7806." Journal of Biological Chemistry 282, no. 7 (2006): 4681–92. http://dx.doi.org/10.1074/jbc.m606986200.

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The cyanobacterium Microcystis aeruginosa is widely known for its production of the potent hepatotoxin microcystin. This cyclic heptapeptide is synthesized non-ribosomally by the thio-template function of a large modular enzyme complex encoded within the 55-kb microcystin synthetase gene (mcy) cluster. The mcy gene cluster also encodes several stand-alone enzymes, putatively involved in the tailoring and export of microcystin. This study describes the characterization of the 2-hydroxy-acid dehydrogenase McyI, putatively involved in the production of d-methyl aspartate at position 3 within the

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42

Wang, Jiang, Yi Yu, Kexuan Tang, et al. "Identification and Analysis of the Biosynthetic Gene Cluster Encoding the Thiopeptide Antibiotic Cyclothiazomycin in Streptomyces hygroscopicus 10-22." Applied and Environmental Microbiology 76, no. 7 (2010): 2335–44. http://dx.doi.org/10.1128/aem.01790-09.

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ABSTRACT Thiopeptide antibiotics are an important class of natural products resulting from posttranslational modifications of ribosomally synthesized peptides. Cyclothiazomycin is a typical thiopeptide antibiotic that has a unique bridged macrocyclic structure derived from an 18-amino-acid structural peptide. Here we reported cloning, sequencing, and heterologous expression of the cyclothiazomycin biosynthetic gene cluster from Streptomyces hygroscopicus 10-22. Remarkably, successful heterologous expression of a 22.7-kb gene cluster in Streptomyces lividans 1326 suggested that there is a minim

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43

Marín, Laura, Elisa M. Miguélez, Claudio J. Villar, and Felipe Lombó. "Bioavailability of Dietary Polyphenols and Gut Microbiota Metabolism: Antimicrobial Properties." BioMed Research International 2015 (2015): 1–18. http://dx.doi.org/10.1155/2015/905215.

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Polyphenolic compounds are plant nutraceuticals showing a huge structural diversity, including chlorogenic acids, hydrolyzable tannins, and flavonoids (flavonols, flavanones, flavan-3-ols, anthocyanidins, isoflavones, and flavones). Most of them occur as glycosylated derivatives in plants and foods. In order to become bioactive at human body, these polyphenols must undergo diverse intestinal transformations, due to the action of digestive enzymes, but also by the action of microbiota metabolism. After elimination of sugar tailoring (generating the corresponding aglycons) and diverse hydroxyl m

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44

Ma, Junying, Zhongwen Wang, Hongbo Huang, et al. "Biosynthesis of Himastatin: Assembly Line and Characterization of Three Cytochrome P450 Enzymes Involved in the Post-tailoring Oxidative Steps." Angewandte Chemie 123, no. 34 (2011): 7943–48. http://dx.doi.org/10.1002/ange.201102305.

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45

Daum, Martina, Iris Peintner, Anton Linnenbrink, et al. "Organisation of the Biosynthetic Gene Cluster and Tailoring Enzymes in the Biosynthesis of the Tetracyclic Quinone Glycoside Antibiotic Polyketomycin." ChemBioChem 10, no. 6 (2009): 1073–83. http://dx.doi.org/10.1002/cbic.200800823.

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46

Ma, Junying, Zhongwen Wang, Hongbo Huang, et al. "Biosynthesis of Himastatin: Assembly Line and Characterization of Three Cytochrome P450 Enzymes Involved in the Post-tailoring Oxidative Steps." Angewandte Chemie International Edition 50, no. 34 (2011): 7797–802. http://dx.doi.org/10.1002/anie.201102305.

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47

Kopp, Florian, Uwe Linne, Markus Oberthür, and Mohamed A. Marahiel. "Harnessing the Chemical Activation Inherent to Carrier Protein-Bound Thioesters for the Characterization of Lipopeptide Fatty Acid Tailoring Enzymes." Journal of the American Chemical Society 130, no. 8 (2008): 2656–66. http://dx.doi.org/10.1021/ja078081n.

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48

Santos-Aberturas, Javier, Jennifer Engel, Jonathan Dickerhoff, et al. "Exploration of the Substrate Promiscuity of Biosynthetic Tailoring Enzymes as a New Source of Structural Diversity for Polyene Macrolide Antifungals." ChemCatChem 7, no. 3 (2014): 490–500. http://dx.doi.org/10.1002/cctc.201402773.

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49

Magarvey, Nathan A., Brad Haltli, Min He, Michael Greenstein, and John A. Hucul. "Biosynthetic Pathway for Mannopeptimycins, Lipoglycopeptide Antibiotics Active against Drug-Resistant Gram-Positive Pathogens." Antimicrobial Agents and Chemotherapy 50, no. 6 (2006): 2167–77. http://dx.doi.org/10.1128/aac.01545-05.

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ABSTRACT The mannopeptimycins are a novel class of lipoglycopeptide antibiotics active against multidrug-resistant pathogens with potential as clinically useful antibacterials. This report is the first to describe the biosynthesis of this novel class of mannosylated lipoglycopeptides. Included here are the cloning, sequencing, annotation, and manipulation of the mannopeptimycin biosynthetic gene cluster from Streptomyces hygroscopicus NRRL 30439. Encoded by genes within the mannopeptimycin biosynthetic gene cluster are enzymes responsible for the generation of the hexapeptide core (nonribosoma

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Helfrich, Eric J. N., Geng-Min Lin, Christopher A. Voigt, and Jon Clardy. "Bacterial terpene biosynthesis: challenges and opportunities for pathway engineering." Beilstein Journal of Organic Chemistry 15 (November 29, 2019): 2889–906. http://dx.doi.org/10.3762/bjoc.15.283.

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Abstract:

Terpenoids are the largest and structurally most diverse class of natural products. They possess potent and specific biological activity in multiple assays and against diseases, including cancer and malaria as notable examples. Although the number of characterized terpenoid molecules is huge, our knowledge of how they are biosynthesized is limited, particularly when compared to the well-studied thiotemplate assembly lines. Bacteria have only recently been recognized as having the genetic potential to biosynthesize a large number of complex terpenoids, but our current ability to associate genet

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