Ketoreductase polypeptides for the production of (R)-3-hydroxythiolane
US-9932615-B2 · Apr 3, 2018 · US
Ketoreductase polypeptides for the production of (R)-3-hydroxythiolane
US10851397B2 · US · B2
| Field | Value |
|---|---|
| Publication number | US-10851397-B2 |
| Application number | US-201916457396-A |
| Country | US |
| Kind code | B2 |
| Filing date | Jun 28, 2019 |
| Priority date | Aug 24, 2007 |
| Publication date | Dec 1, 2020 |
| Grant date | Dec 1, 2020 |
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Abstract
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The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.
First claim
Opening claim text (preview).
What is claimed is: 1. An engineered polynucleotide encoding an engineered ketoreductase polypeptide, wherein the engineered ketoreductase polypeptide comprises an amino acid sequence that is at least 90% identical to the reference sequence SEQ ID NO:4, and wherein said amino acid sequence comprises a valine or threonine at position 94. 2. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises one or more additional substitutions selected from: the residue corresponding to X3 is asparagine, aspartic acid, or tyrosine; the residue corresponding to X7 is glycine, histidine, serine or asparagine; the residue corresponding to X11 is isoleucine or threonine; the residue corresponding to X16 is threonine, alanine, valine, or glycine; the residue corresponding to X19 is isoleucine or valine; the residue corresponding to X23 is isoleucine or phenylalanine; the residue corresponding to X41 is serine, alanine, or valine; the residue corresponding to X45 is glutamic acid or glycine; the residue corresponding to X49 is lysine or arginine; the residue corresponding to X57 is isoleucine or valine; the residue corresponding to X60 is phenylalanine, valine, or threonine; the residue corresponding to X64 is alanine, serine, or threonine; the residue corresponding to X72 is lysine or arginine, particularly arginine; the residue corresponding to X82 is glycine or serine; the residue corresponding to X95 is valine or alanine; the residue corresponding to X96 is asparagine, serine, proline, alanine, or glutamic acid; the residue corresponding to X97 is lysine, arginine or leucine; the residue corresponding to X106 is glutamic acid or aspartic acid; the residue corresponding to X108 is arginine or histidine; the residue corresponding to X111 is leucine or methionine; the residue corresponding to X117 is glycine or serine; the residue corresponding to X126 is isoleucine or valine; the residue corresponding to X127 is glutamine or arginine; the residue corresponding to X145 is aspartic acid or serine; the residue corresponding to X147 is phenylalanine, leucine or serine; the residue corresponding to X152 is threonine, serine, or methionine; the residue corresponding to X157 is asparagine, glutamine, threonine, serine, or aspartic acid; the residue corresponding to X163 is valine or isoleucine; the residue corresponding to X173 is aspartic acid or glycine; the residue corresponding to X177 is lysine or arginine; the residue corresponding to X192 is lysine, arginine or glutamic acid; the residue corresponding to X194 is proline, glycine, aspartic acid, arginine, or leucine; the residue corresponding to X198 is aspartic acid or glycine; the residue corresponding to X200 is proline, glutamic acid, or lysine; the residue corresponding to X206 is methionine or glutamine; the residue corresponding to X208 is glutamine, histidine or arginine; the residue corresponding to X210 is threonine or alanine; the residue corresponding to X211 is lysine or glutamic acid; the residue corresponding to X214 is methionine, valine or threonine, or serine; the residue corresponding to X217 is isoleucine or phenylalanine; the residue corresponding to X223 is isoleucine or valine; and the residue corresponding to X226 is isoleucine or valine. 3. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , wherein the ketoreductase polypeptide amino acid sequence further comprises at least one additional substitution selected from: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X96 is a constrained, aliphatic, non-polar, acidic, or polar residue; the residue corresponding to X108 is a basic, constrained, or aromatic residue; the residue corresponding to X117 is a non-polar or polar residue; the residue corresponding to X147 is a non-polar or alphatic residue; the residue corresponding to X157 is a polar or acidic residue; the residue corresponding to X173 is an acidic or non-polar residue; the residue corresponding to X206 is a polar or non-polar residue; and the residue corresponding to X223 is an aliphatic or non-polar residue. 4. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises the following substitutions: the residue corresponding to X117 is a non-polar or polar residue; the residue corresponding to X147 is a non-polar or alphatic residue; the residue corresponding to X157 is a polar or acidic residue. 5. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises at least one substitution selected from: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X108 is a basic, constrained, or aromatic residue; the residue corresponding to X117 is a non-polar or polar residue, particularly serine; the residue corresponding to X147 is a non-polar or alphatic residue; the residue corresponding to X157 is a polar or acidic residue, particularly a threonine. 6. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence comprises the following substitutions: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X96 is a constrained, aliphatic, non-polar, acidic, or polar residue; the residue corresponding to X108 is a basic, constrained, or aromatic residue; the residue corresponding to X117 is a non-polar or polar residue, partcularly serine; the residue corresponding to X147 is leucine; and the residue corresponding to X157 is a polar or acidic residue, particularly threonine. 7. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises the following substitutions: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X96 is a constrained, aliphatic, non-polar, acidic, or polar residue; residue corresponding to X108 is a basic, constrained, or constrained residue; the residue corresponding to X117 is a non-polar or polar residue, particularly serine; the residue corresponding to X157 is a polar or acidic residue, particularly a threonine. 8. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises the following substitutions: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X108 is a basic, constrained, or aromatic residue; the residue corresponding to X117 is a non-polar or polar residue; the residue corresponding to X157 is a polar or acidic residue; and the residue corresponding to X206 is a polar or non-polar residue. 9. The engineered polynucleotide encoding the engineered ketoreductase polypeptide of claim 1 , in which the ketoreductase polypeptide amino acid sequence further comprises at least one of the following substitutions: the residue corresponding to X7 is a non-polar, polar, or constrained residue; the residue corresponding to X96 is a constrained, aliphatic, non-polar, acidic, or polar residue; the residue corresponding to X108 is a basic, constrained, or aromatic residue; the residue co
Assignees
Inventors
Classifications
acting on CH-OH groups as donors (1.1) · CPC title
using catalysts, e.g. selective catalysts · CPC title
Carbonyl reductase (NADPH) (1.1.1.184) · CPC title
Heterorings having sulfur atoms as ring heteroatoms, e.g. vitamin B1, thiamine nucleus and open chain analogs · CPC title
- C12P17/00Primary
Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms (C12P13/04 - C12P13/24 take precedence) · CPC title
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- What does patent US10851397B2 cover?
- The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compo…
- Who is the assignee on this patent?
- Codexis Inc
- What technology area does this patent fall under?
- Primary CPC classification C12P17/00. Mapped technology areas include Chemistry & Metallurgy.
- When was this patent published?
- Publication date Tue Dec 01 2020 00:00:00 GMT+0000 (Coordinated Universal Time) (B2). Legal status and post-grant events are not shown on this page.
- What related patents are in patentsdb?
- We list 3 related publications on this page (citations in our corpus or others sharing the same primary CPC).