Microbial and Enzymatic Processes for the Production of Biologically and Chemically Useful Compounds [New Synthetic Methods (69)]

Yamada, Hideaki; Shimizu, Sakayu

doi:10.1002/anie.198806221

Cited by 187 publications

(15 citation statements)

References 220 publications

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“…78 The bulk of esterase-mediated reactions have been conducted with porcine liver esterase (PLE; also called porcine liver carboxyesterase) and its applicability is restricted to reactions performed in aqueous media. 79 PLE was first demonstrated to generate dipeptides with N-protected amino acid esters (Table 3), 80 and subsequently this enzyme was shown to catalyze intramolecular amide bond formation from γ-amino esters in water to give a mixture of the γ-lactam and the hydrolysis product. 81 Similar results were observed using PLE with the ‘degradation’ of racemic ethyl 4-phenyl-4-aminobutanoate, where the stereoselective formation of ( S )-5-phenyl-2-pyrrolidine was observed alongside the hydrolysis product (Figure 8).…”

Section: Transacylationmentioning

confidence: 99%

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

2015

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Amide bond-containing (ABC) biomolecules are some of the most intriguing and functionally significant natural products with unmatched utility in medicine, agriculture and biotechnology. The enzymatic formation of an amide bond is therefore a particularly interesting platform for engineering the synthesis of structurally diverse natural and unnatural ABC molecules for applications in drug discovery and molecular design. As such, efforts to unravel the mechanisms involved in carboxylate activation and substrate selection has led to the characterization of a number of structurally and functionally distinct protein families involved in amide bond synthesis. Unlike ribosomal synthesis and thio-templated synthesis using nonribosomal peptide synthetases, which couple the hydrolysis of phosphoanhydride bond(s) of ATP and proceed via an acyl-adenylate intermediate, here we discuss two mechanistically alternative strategies: ATP-dependent enzymes that generate acylphosphate intermediates and ATP-independent transacylation strategies. Several examples highlighting the function and synthetic utility of these amide bond-forming strategies are provided.

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Section: Transacylationmentioning

confidence: 99%

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

2015

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“…Further details are available in earlier works 3,5,7,17 where the immobilization techniques are also substantiated.…”

Section: Methodsmentioning

confidence: 97%

Evaluation of In Situ Electroenzymatic Regeneration of Coenzyme NADH in Packed Bed Membrane Reactors

Chen

Fenton

Fisher

et al. 2004

J. Electrochem. Soc.

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Characterization of our electroenzymatic membrane reactors with respect to transport and reaction processes has been accomplished. Both batch and flow configurations were evaluated using the biosynthesis of lactate from pyruvate as a model system. A key feature is the in situ regeneration of the coenzyme nicotinamide adenine dinucleotide ͑NADH͒. Cyclic voltammetry was used to investigate the mechanisms present in the free solution and on porous enzyme immobilized, graphite electrodes. These results were essential for the design and evaluation of the flow-by electrode and subsequent reactor performance studies. The electrodes utilize an immobilized enzyme system ͓lipoamide dehydrogenase ͑LipDH͒ and methyl viologen as a mediator͔ within porous graphite cathodes, encapsulated by a cation exchange membrane ͑Nafion 124, DuPont͒. The free flowing fluid contains the pyruvate/lactate ͑and coproducts͒, the enzyme lactate dehydrogenase ͑LDH͒ and the coenzyme NADH/NAD ϩ system. Lactate yields up to 70% were obtained when the reactor system was operated in a semibatch ͑i.e., recirculation͒ mode for 24 h, as compared to only 50% when operated in a simple batch mode for 200 h. The multipass operating scheme permits optimization studies to be conducted on system parameters. Operating regimes where either mass transfer or kinetics control the process synthesis were identified by flow perturbation studies.In many biosynthesis processes, a coenzyme is required in combination with the base enzyme to function as a high efficiency catalyst. Nicotinamide adenine dinucleotide ͓NAD͑H͔͒ is one such coenzyme, participating in redox reaction syntheses. A regenerating system is needed for the recycling of this coenzyme to reduce operating costs in continuous in vitro synthesis processes, mimicking the in vivo regeneration process. Much effort has focused on improving this regeneration process with electrochemical methods receiving increased attention. 1 Direct regeneration on an electrode has proven to be extremely difficult. 2 To produce enzymatically active NADH by an electrochemical method, either acceleration of protonation or inhibition of intermolecular coupling of NAD ϩ is required. Redox mediators permit the coupling of electrochemical and enzymatic reactions resulting in acceleration. The mediator accepts electrons from the electrode and transfers them to the coenzyme via an enzymatic reaction, and an electron transfer chain is thus established. An example, as demonstrated in our laboratory, is the synthesis of lactate using our biomimetic membranes. 3 The regenerated coenzyme is recycled during he biosynthesis process, demonstrating its viability and versatility. 3,4 Enzyme-coated electrodes were first used for chemical analysis because the media is not perturbed as it is in conventional methods for continuous or serial analysis of enzymes. 5,6 The immobilization of mediator and enzyme on electrodes can reduce the separation procedure, increase the selectivity of enzymatic synthesis, 7 and stabilize the enzyme activity. 8,9 Variou...

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“…Potential applications of biocatalysts are reviewed by Rosazza (1982), Whitesides (1985), Soda & Yonaha (1987) and Yamada & Shimizu (1988). Vinegar, a product of the microbial oxidation of ethanol, was recorded in the Bible, and the trickling process for vinegar manufacture, devised around 1815, was an early use of immobilized cells.…”

Section: The Importance Of Biocatalystsmentioning

confidence: 99%

Microbial Enzymes and Biotechnology

Fogarty¹,

Kelly²

1990

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Microbial and Enzymatic Processes for the Production of Biologically and Chemically Useful Compounds [New Synthetic Methods (69)]

Cited by 187 publications

References 220 publications

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

Evaluation of In Situ Electroenzymatic Regeneration of Coenzyme NADH in Packed Bed Membrane Reactors

Microbial Enzymes and Biotechnology

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