Oscar Alvizo
Research Subjects
Oscar Alvizo has a total of 47 co-authors. Here are the top co-authors by number of shared publications:
- Anupam P. Gohel
Codexis, Inc., 200 Penobscot Drive, Redwood City, CA, 94063, USA
2 shared publications - Birgit Kosjek
Process Research and Development Merck & Co., Inc. Rahway NJ 07065 USA
2 shared publications - Derek J. Smith
Codexis, Inc., 200 Penobscot Drive, Redwood City, CA, 94063, USA
2 shared publications - Fabien L. Cabirol
Codexis, Inc., 200 Penobscot Drive, Redwood City, CA, 94063, USA
2 shared publications - Feng Xu
Department of Process Research, Merck Research Laboratory, Rahway, New Jersey 07065, USA
2 shared publications - Haibin Chen
Codexis, Inc., 200 Penobscot Drive, Redwood City, CA, 94063, USA
2 shared publications
Latest Publications
- Open Access
- 26 October 2023
- Published by American Chemical Society (ACS) in ChemRxiv
Development of a Biocatalytic Aerobic Oxidation for the Manufacturing Route to Islatravir
Biocatalytic oxidations have the potential to address many synthetic chemistry challenges, enabling the selective synthesis of chiral intermediates such as carbonyl compounds, alcohols, or amines. The use of oxygen-dependent enzymes can dramatically reduce the environmental footprint of redox transformations at manufacturing scale. Here, as part of the biocatalytic cascade to an anti-HIV investigational drug islatravir 1, we describe the development of an aerobic oxidation process delivering (R)-ethynylglyceraldehyde 3-phosphate 3 using an evolved galactose oxidase enzyme. Integrated enzyme and reaction engineering were critical for achieving a robust, high-yielding oxidation performed at pilot plant scale (>20 kg, 90% yield).
- 26 October 2023
- Published by American Chemical Society (ACS) in ChemRxiv
Open AccessDevelopment of a Biocatalytic Aerobic Oxidation for the Manufacturing Route to Islatravir
Biocatalytic oxidations have the potential to address many synthetic chemistry challenges, enabling the selective synthesis of chiral intermediates such as carbonyl compounds, alcohols, or amines. The use of oxygen-dependent enzymes can dramatically reduce the environmental footprint of redox transformations at manufacturing scale. Here, as part of the biocatalytic cascade to an anti-HIV investigational drug islatravir 1, we describe the development of an aerobic oxidation process delivering (R)-ethynylglyceraldehyde 3-phosphate 3 using an evolved galactose oxidase enzyme. Integrated enzyme and reaction engineering were critical for achieving a robust, high-yielding oxidation performed at pilot plant scale (>20 kg, 90% yield).
- 3 May 2018
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 57 (23) , 6863-6867
Synthesis of Vibegron Enabled by a Ketoreductase Rationally Designed for High pH Dynamic Kinetic Reduction
Described here is an efficient stereoselective synthesis of vibegron enabled by an enzymatic dynamic kinetic reduction that proceeds in a high‐pH environment. To overcome enzyme performance limitations under these conditions, a ketoreductase was evolved by a computationally and structurally aided strategy to increase cofactor stability through tighter binding.
- 3 May 2018
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 57 (23) , 6863-6867
Synthesis of Vibegron Enabled by a Ketoreductase Rationally Designed for High pH Dynamic Kinetic Reduction
Described here is an efficient stereoselective synthesis of vibegron enabled by an enzymatic dynamic kinetic reduction that proceeds in a high‐pH environment. To overcome enzyme performance limitations under these conditions, a ketoreductase was evolved by a computationally and structurally aided strategy to increase cofactor stability through tighter binding.
- 3 May 2018
- Published by Wiley in Angewandte Chemie
- Vol. 130 (23) , 6979-6983
Synthesis of Vibegron Enabled by a Ketoreductase Rationally Designed for High pH Dynamic Kinetic Reduction
Described here is an efficient stereoselective synthesis of vibegron enabled by an enzymatic dynamic kinetic reduction that proceeds in a high‐pH environment. To overcome enzyme performance limitations under these conditions, a ketoreductase was evolved by a computationally and structurally aided strategy to increase cofactor stability through tighter binding.
- 3 May 2018
- Published by Wiley in Angewandte Chemie
- Vol. 130 (23) , 6979-6983
Synthesis of Vibegron Enabled by a Ketoreductase Rationally Designed for High pH Dynamic Kinetic Reduction
Described here is an efficient stereoselective synthesis of vibegron enabled by an enzymatic dynamic kinetic reduction that proceeds in a high‐pH environment. To overcome enzyme performance limitations under these conditions, a ketoreductase was evolved by a computationally and structurally aided strategy to increase cofactor stability through tighter binding.
- 3 November 2014
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 111 (46) , 16436-16441
Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas
Significance: It is clear that to address climate change, the amount of CO2released into the atmosphere by industrial processes has to be reduced. Carbonic anhydrase regulates CO2in nearly every single living organism and is one of the most efficient enzymes in nature. To leverage that efficiency, a β-class carbonic anhydrase was engineered using directed evolution to withstand some of the harshest conditions associated with an industrial carbon capture process. The approach laid out can be generally applied in the development of natural enzymes for their use in industrial applications.
- 3 November 2014
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 111 (46) , 16436-16441
Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas
Significance: It is clear that to address climate change, the amount of CO2released into the atmosphere by industrial processes has to be reduced. Carbonic anhydrase regulates CO2in nearly every single living organism and is one of the most efficient enzymes in nature. To leverage that efficiency, a β-class carbonic anhydrase was engineered using directed evolution to withstand some of the harshest conditions associated with an industrial carbon capture process. The approach laid out can be generally applied in the development of natural enzymes for their use in industrial applications.