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Truppo M.D.,University of Manchester | David Rozzell J.,Codexis Inc. | Turner N.J.,University of Manchester
Organic Process Research and Development | Year: 2010

Two methods for the efficient (50 g/L) production of optically pure amines from their corresponding ketones using transaminases have been developed. The first method utilizes an ion-exchange resin for in situ product removal allowing the reaction to be carried out a substrate concentration of 50 g/L. The second approach relies upon conversion of the initially formed amine, via spontaneous cyclisation, to a noninhibitory product. Both methods have been demonstrated at 50 mL scale. (R)- and (S)-methylbenzylamine, and (R)- and (S)-6-methyl-2- piperidone have been produced in >90% isolated yield and >99% ee. © 2010 American Chemical Society. Source


Huisman G.W.,Codexis Inc. | Collier S.J.,Codexis
Current Opinion in Chemical Biology | Year: 2013

Biocatalysis has established itself as a scalable and green technology for the production of a broad range of pharmaceutical APIs and intermediates. The number and scope of biocatalysts employed on large scale to deliver cost-advantaged and quality-advantaged processes to important substances continue to expand. This review discusses the recent developments in the field, including examples of processes leveraging hydrolases, reductases, transaminases, oxidases and other biocatalysts, focused on the preparation of important investigational and launched therapeutics. Biocatalysts recently discovered, and in some cases rediscovered, for the interesting chemistry they enable are likely to further substantiate the expansion of the biocatalysis field. © 2013 Elsevier Ltd. Source


Biondi E.,University of Missouri | Nickens D.G.,Indiana University Bloomington | Warren S.,University of Missouri | Saran D.,Indiana University Bloomington | And 2 more authors.
Nucleic Acids Research | Year: 2010

Accommodation of donor and acceptor substrates is critical to the catalysis of (thio)phosphoryl group transfer, but there has been no systematic study of donor nucleotide recognition by kinase ribozymes, and there is relatively little known about the structural requirements for phosphorylating internal 2′OH. To address these questions, new self-phosphorylating ribozymes were selected that utilize ATP(gammaS) or GTP(gammaS) for 2′OH (thio)phosphorylation. Eight independent sequence families were identified among 57 sequenced isolates. Kinetics, donor nucleotide recognition and secondary structures were analyzed for representatives from each family. Each ribozyme was highly specific for its cognate donor. Competition assays with nucleotide analogs showed a remarkable convergence of donor recognition requirements, with critical contributions to recognition provided by the Watson-Crick face of the nucleobase, lesser contributions from donor nucleotide ribose hydroxyls, and little or no contribution from the Hoogsteen face. Importantly, most ribozymes showed evidence of significant interaction with one or more donor phosphates, suggesting that-unlike most aptamers-these ribozymes use phosphate interactions to orient the gamma phosphate within the active site for in-line displacement. All but one of the mapped (thio)phosphorylation sites are on unpaired guanosines within internal bulges. Comparative structural analysis identified three loosely-defined consensus structural motifs for kinase ribozyme active sites. © The Author(s) 2010. Published by Oxford University Press. Source


Patent
Codexis Inc. | Date: 2015-04-13

The present disclosure provides engineered transaminase enzymes having improved properties as compared to a naturally occurring wild-type transaminase enzyme. Also provided are polynucleotides encoding the engineered transaminase enzymes, host cells capable of expressing the engineered transaminase enzymes, and methods of using the engineered transaminase enzymes to synthesize a variety of chiral compounds.


Patent
Codexis Inc. | Date: 2013-06-18

The present disclosure provides engineered transaminase enzymes having improved properties as compared to a naturally occurring wild-type transaminase enzyme. Also provided are polynucleotides encoding the engineered transaminase enzymes, host cells capable of expressing the engineered transaminase enzymes, and methods of using the engineered transaminase enzymes to synthesize a variety of chiral compounds.

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