Acetohydroxyacid synthase: A new enzyme for chiral synthesis of R-phenylacetylcarbinol
We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of (R)‐phenylacetylcarbinol (R‐PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)‐acetohydroxyacids from...
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| Published in | Biotechnology and bioengineering Vol. 83; no. 7; pp. 833 - 840 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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Hoboken
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30.09.2003
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| Abstract | We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of (R)‐phenylacetylcarbinol (R‐PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)‐acetohydroxyacids from pyruvate and a second ketoacid. (R)‐phenylacetylcarbinol is the precursor of important drugs having α and β adrenergic properties, such as L‐ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole‐cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 83: 833–840, 2003. |
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| AbstractList | We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of (R)‐phenylacetylcarbinol (R‐PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)‐acetohydroxyacids from pyruvate and a second ketoacid. (R)‐phenylacetylcarbinol is the precursor of important drugs having α and β adrenergic properties, such as L‐ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole‐cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 83: 833–840, 2003. We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (=>98% enantiomeric excess) synthesis of (R)- phenylacetylcarbinol (R-PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)-acetohydroxyacids from pyruvate and a second ketoacid. (R)-phenylacetylcarbinol is the precursor of important drugs having alpha and beta adrenergic properties, such as L-ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole-cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (> or =98% enantiomeric excess) synthesis of (R)-phenylacetylcarbinol (R-PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)-acetohydroxyacids from pyruvate and a second ketoacid. (R)-phenylacetylcarbinol is the precursor of important drugs having alpha and beta adrenergic properties, such as L-ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole-cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used.We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (> or =98% enantiomeric excess) synthesis of (R)-phenylacetylcarbinol (R-PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)-acetohydroxyacids from pyruvate and a second ketoacid. (R)-phenylacetylcarbinol is the precursor of important drugs having alpha and beta adrenergic properties, such as L-ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole-cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of ( R )‐phenylacetylcarbinol (R‐PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of ( S )‐acetohydroxyacids from pyruvate and a second ketoacid. ( R )‐phenylacetylcarbinol is the precursor of important drugs having α and β adrenergic properties, such as L ‐ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole‐cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 83: 833–840, 2003. We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (> or =98% enantiomeric excess) synthesis of (R)-phenylacetylcarbinol (R-PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)-acetohydroxyacids from pyruvate and a second ketoacid. (R)-phenylacetylcarbinol is the precursor of important drugs having alpha and beta adrenergic properties, such as L-ephedrine, pseudoephedrine, and norephedrin. It is currently produced by whole-cell fermentations, but the use of the isolated enzyme pyruvate decarboxylase (PDC) for this purpose is the subject of active research and development efforts. Some of the AHAS isozymes of Escherichia coli have important advantages compared to PDC, including negligible acetaldehyde formation and high conversion of substrates (both pyruvate and benzaldehyde) to PAC. Acetohydroxyacid synthase isozyme I is particularly efficient. The reaction is not limited to condensation of pyruvate with benzaldehyde and other aromatic aldehydes may be used. |
| Author | Vyazmensky, Maria Barak, Ze'ev Chipman, David M. Geresh, Shimona Engel, Stanislav |
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| Keywords | chiral Enzyme thiamin diphosphate Benzaldehyde Lyases enantiomeric excess pyruvate biocatalysis Biocatalyst Oxo-acid-lyases Carbon-carbon lyases Carboxy-lyases Chirality Acetolactate synthase Stereospecificity hydroxyketone Pyruvate decarboxylase |
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| References | Breuer M, Pohl M, Hauere B, Lingen B. 2002. High-throughput assay of (R)-phenylacetylcarbinol synthesized by pyruvate decarboxylase. Anal Bioanal Chem 374:1069-1073. Rogers PL, Shin HS, Wang B. 1997. Biotransformation for L-ephedrine production. Adv Biochem Eng Biotechnol 56:33-59. Crout DHG, Lee ER, Rathbone DL. 1990. Absolute configuration of the product of the acetolactate synthase reaction by a novel method of analysis using acetolactate decarboxylase. J Chem Soc-Perkin Trans 1 1:1367-1370. Epelbaum S, Chipman DM, Barak Z. 1990. Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited. Anal Biochem 191:96-99. Brusee J, Roos EC, Der Gen AV. 1988. Bio-organic synthesis of optically active cyanohydrins and acyloins. Tetrahedron Lett 29:4485-4488. Ibdah M, Bar-Ilan A, Livnah O, Schloss JV, Barak Z, Chipman DM. 1996. Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis. Biochemistry 35:16282-16291. Bar-Ilan A, Balan V, Tittmann K, Golbik R, Vyazmensky M, Hubner G, Barak Z, Chipman DM. 2001. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 40:11946-11954. Bornemann S, Crout DHG, Dalton H, Kren V, Lobell M, Dean G, Thomson N, Turner MM. 1996. Stereospecific formation of R-aromatic acyloins by Zymomonas mobilis pyruvate decarboxylase. J Chem Soc-Perkin Trans 1 5:425-430. Hanc O, Karac B. 1956. Yeast carboxylase and the formation of phenylacetylcarbinol. Naturwissenschaften 43:498-501. Iding H, Siegert P, Mesch K, Pohl M. 1998. Application of α-keto acid decarboxylases in biotransformations. Biochim Biophys Acta 1385:307-322. Krampitz LO. 1948. Preparation and determination of 2-acetolactic acid. Arch Biochem 17:81. Bradford M. 1976. A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248. Kren V, Crout DHG, Dalton H, Hutchinson DW, Konig W, Turner MM, Dean G, Thomson N. 1993. Pyruvate decarboxylase-A new enzyme for the production of acyloins by biotransformation. J Chem Soc-Chem Commun 341-343. Chipman D, Barak Z, Schloss JV. 1988. Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases. Biochim Biophys Acta 1385:401-419. Stetter H, Dambkes G. 1977. Uber die praparative Nutzung der Thiazoliumsalz-katalysierten Acyloinund Benzoin-Bildung; II. Herstellung unsymmetrischer Acyloine and α-Diletone. Synthesis 403-404. Bruhn H, Pohl M, Grotzinger J, Kula MR. 1995. The replacement of Trp392 by alanine influences the decarboxylase/carboligase activity and stability of pyruvate decarboxylase from Zymomonas mobilis. Eur J Biochem 234:650-655. Pohl M. 1997. Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis. Adv Biochem Eng Biotechnol 58:15-43. Shukla VB, Kulkarni PR. 2000. L-Phenylacetylcarbinol (L-PAC): biosynthesis and industrial applications. World J Microbiol Biotechnol 16:499-506. Iwan P, Goetz G, Schmitz S, Hauer B, Breuer M, Pohl M. 2001. Studies on the continuous production of (R)-(-)-phenylacetylcarbinol in an enzyme-membrane reactor. J Mol Catal B-Enz 11:387-396. Schorken U, Sprenger GA. 1998. Thiamin-dependent enzymes as catalysts in chemoenzymatic syntheses. Biochim Biophys Acta 1385:229-243. Ward OP, Singh A. 2000. Enzymatic asymmetric synthesis by decarboxylases. Curr Opin Biotechnol 11:520-526. Vyazmensky M, Elkayam T, Chipman DM, Barak Z. 2000. Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Meth Enzymol 324:95-103. 1990; 1 1987; l 2000; 16 2001 1988; 29 1990 2002; 374 2000; 324 1976; 72 1956; 43 1997; 58 2000; 11 1997; 56 1990; 191 1995; 234 1993 1998; 1385 2001; 11 1996; 5 1996; 35 2001; 40 1988; 1385 1948; 17 1977 Krampitz LO (e_1_2_1_17_1) 1948; 17 e_1_2_1_20_1 e_1_2_1_23_1 e_1_2_1_24_1 e_1_2_1_22_1 e_1_2_1_27_1 e_1_2_1_26_1 e_1_2_1_7_1 e_1_2_1_8_1 e_1_2_1_5_1 e_1_2_1_6_1 e_1_2_1_3_1 e_1_2_1_12_1 e_1_2_1_4_1 e_1_2_1_13_1 e_1_2_1_2_1 e_1_2_1_11_1 e_1_2_1_16_1 Umbarger HE (e_1_2_1_25_1) 1987 e_1_2_1_14_1 Schloss JV (e_1_2_1_21_1) 1990 Crout DHG (e_1_2_1_10_1) 1990 e_1_2_1_15_1 e_1_2_1_9_1 e_1_2_1_18_1 e_1_2_1_19_1 |
| References_xml | – reference: Vyazmensky M, Elkayam T, Chipman DM, Barak Z. 2000. Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Meth Enzymol 324:95-103. – reference: Crout DHG, Lee ER, Rathbone DL. 1990. Absolute configuration of the product of the acetolactate synthase reaction by a novel method of analysis using acetolactate decarboxylase. J Chem Soc-Perkin Trans 1 1:1367-1370. – reference: Epelbaum S, Chipman DM, Barak Z. 1990. Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited. Anal Biochem 191:96-99. – reference: Bruhn H, Pohl M, Grotzinger J, Kula MR. 1995. The replacement of Trp392 by alanine influences the decarboxylase/carboligase activity and stability of pyruvate decarboxylase from Zymomonas mobilis. Eur J Biochem 234:650-655. – reference: Chipman D, Barak Z, Schloss JV. 1988. Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases. Biochim Biophys Acta 1385:401-419. – reference: Iwan P, Goetz G, Schmitz S, Hauer B, Breuer M, Pohl M. 2001. Studies on the continuous production of (R)-(-)-phenylacetylcarbinol in an enzyme-membrane reactor. J Mol Catal B-Enz 11:387-396. – reference: Krampitz LO. 1948. Preparation and determination of 2-acetolactic acid. Arch Biochem 17:81. – reference: Pohl M. 1997. Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis. Adv Biochem Eng Biotechnol 58:15-43. – reference: Bar-Ilan A, Balan V, Tittmann K, Golbik R, Vyazmensky M, Hubner G, Barak Z, Chipman DM. 2001. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 40:11946-11954. – reference: Schorken U, Sprenger GA. 1998. Thiamin-dependent enzymes as catalysts in chemoenzymatic syntheses. Biochim Biophys Acta 1385:229-243. – reference: Hanc O, Karac B. 1956. Yeast carboxylase and the formation of phenylacetylcarbinol. Naturwissenschaften 43:498-501. – reference: Rogers PL, Shin HS, Wang B. 1997. Biotransformation for L-ephedrine production. Adv Biochem Eng Biotechnol 56:33-59. – reference: Kren V, Crout DHG, Dalton H, Hutchinson DW, Konig W, Turner MM, Dean G, Thomson N. 1993. Pyruvate decarboxylase-A new enzyme for the production of acyloins by biotransformation. J Chem Soc-Chem Commun 341-343. – reference: Bornemann S, Crout DHG, Dalton H, Kren V, Lobell M, Dean G, Thomson N, Turner MM. 1996. Stereospecific formation of R-aromatic acyloins by Zymomonas mobilis pyruvate decarboxylase. J Chem Soc-Perkin Trans 1 5:425-430. – reference: Breuer M, Pohl M, Hauere B, Lingen B. 2002. High-throughput assay of (R)-phenylacetylcarbinol synthesized by pyruvate decarboxylase. Anal Bioanal Chem 374:1069-1073. – reference: Stetter H, Dambkes G. 1977. Uber die praparative Nutzung der Thiazoliumsalz-katalysierten Acyloinund Benzoin-Bildung; II. Herstellung unsymmetrischer Acyloine and α-Diletone. Synthesis 403-404. – reference: Brusee J, Roos EC, Der Gen AV. 1988. Bio-organic synthesis of optically active cyanohydrins and acyloins. Tetrahedron Lett 29:4485-4488. – reference: Bradford M. 1976. A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248. – reference: Iding H, Siegert P, Mesch K, Pohl M. 1998. Application of α-keto acid decarboxylases in biotransformations. Biochim Biophys Acta 1385:307-322. – reference: Ibdah M, Bar-Ilan A, Livnah O, Schloss JV, Barak Z, Chipman DM. 1996. Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis. Biochemistry 35:16282-16291. – reference: Ward OP, Singh A. 2000. Enzymatic asymmetric synthesis by decarboxylases. Curr Opin Biotechnol 11:520-526. – reference: Shukla VB, Kulkarni PR. 2000. L-Phenylacetylcarbinol (L-PAC): biosynthesis and industrial applications. World J Microbiol Biotechnol 16:499-506. – volume: 40 start-page: 11946 year: 2001 end-page: 11954 article-title: Binding and activation of thiamin diphosphate in acetohydroxyacid synthase publication-title: Biochemistry – volume: 35 start-page: 16282 year: 1996 end-page: 16291 article-title: Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site‐directed mutagenesis publication-title: Biochemistry – volume: 1385 start-page: 229 year: 1998 end-page: 243 article-title: Thiamin‐dependent enzymes as catalysts in chemoenzymatic syntheses publication-title: Biochim Biophys Acta – volume: 1 start-page: 1367 year: 1990 end-page: 1370 article-title: Absolute configuration of the product of the acetolactate synthase reaction by a novel method of analysis using acetolactate decarboxylase publication-title: J Chem Soc‐Perkin Trans 1 – year: 2001 – start-page: 199 year: 1990 end-page: 242 – volume: 17 start-page: 81 year: 1948 article-title: Preparation and determination of 2‐acetolactic acid publication-title: Arch Biochem – volume: l start-page: 352 year: 1987 – volume: 11 start-page: 387 year: 2001 end-page: 396 article-title: Studies on the continuous production of ( )‐(‐)‐phenylacetylcarbinol in an enzyme‐membrane reactor publication-title: J Mol Catal B‐Enz – volume: 72 start-page: 248 year: 1976 article-title: A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding publication-title: Anal Biochem – volume: 43 start-page: 498 year: 1956 end-page: 501 article-title: Yeast carboxylase and the formation of phenylacetylcarbinol publication-title: Naturwissenschaften – volume: 11 start-page: 520 year: 2000 end-page: 526 article-title: Enzymatic asymmetric synthesis by decarboxylases publication-title: Curr Opin Biotechnol – start-page: 341 year: 1993 end-page: 343 article-title: Pyruvate decarboxylase—A new enzyme for the production of acyloins by biotransformation publication-title: J Chem Soc‐Chem Commun – volume: 29 start-page: 4485 year: 1988 end-page: 4488 article-title: Bio‐organic synthesis of optically active cyanohydrins and acyloins publication-title: Tetrahedron Lett – volume: 16 start-page: 499 year: 2000 end-page: 506 article-title: L‐Phenylacetylcarbinol (L‐PAC): biosynthesis and industrial applications publication-title: World J Microbiol Biotechnol – volume: 324 start-page: 95 year: 2000 end-page: 103 article-title: Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme publication-title: Meth Enzymol – start-page: 329 year: 1990 end-page: 356 – volume: 58 start-page: 15 year: 1997 end-page: 43 article-title: Protein design on pyruvate decarboxylase (PDC) by site‐directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis publication-title: Adv Biochem Eng Biotechnol – volume: 5 start-page: 425 year: 1996 end-page: 430 article-title: Stereospecific formation of ‐aromatic acyloins by pyruvate decarboxylase publication-title: J Chem Soc‐Perkin Trans 1 – volume: 1385 start-page: 401 year: 1988 end-page: 419 article-title: Biosynthesis of 2‐aceto‐2‐hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases publication-title: Biochim Biophys Acta – volume: 234 start-page: 650 year: 1995 end-page: 655 article-title: The replacement of Trp392 by alanine influences the decarboxylase/carboligase activity and stability of pyruvate decarboxylase from publication-title: Eur J Biochem – volume: 191 start-page: 96 year: 1990 end-page: 99 article-title: Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited publication-title: Anal Biochem – volume: 1385 start-page: 307 year: 1998 end-page: 322 article-title: Application of α‐keto acid decarboxylases in biotransformations publication-title: Biochim Biophys Acta – volume: 56 start-page: 33 year: 1997 end-page: 59 article-title: Biotransformation for L‐ephedrine production publication-title: Adv Biochem Eng Biotechnol – start-page: 403 year: 1977 end-page: 404 article-title: Uber die praparative Nutzung der Thiazoliumsalz‐katalysierten Acyloinund Benzoin‐Bildung; II. Herstellung unsymmetrischer Acyloine and α‐Diletone publication-title: Synthesis – volume: 374 start-page: 1069 year: 2002 end-page: 1073 article-title: High‐throughput assay of ( )‐phenylacetylcarbinol synthesized by pyruvate decarboxylase publication-title: Anal Bioanal Chem – ident: e_1_2_1_12_1 doi: 10.1016/0003-2697(90)90393-N – start-page: 329 volume-title: Biosynthesis of Branched Chain Amino Acids year: 1990 ident: e_1_2_1_21_1 – ident: e_1_2_1_6_1 doi: 10.1007/s00216-002-1579-1 – ident: e_1_2_1_15_1 doi: 10.1016/S0167-4838(98)00076-4 – ident: e_1_2_1_20_1 doi: 10.1007/BFb0103029 – ident: e_1_2_1_14_1 doi: 10.1021/bi961588i – ident: e_1_2_1_18_1 doi: 10.1039/c39930000341 – volume: 17 start-page: 81 year: 1948 ident: e_1_2_1_17_1 article-title: Preparation and determination of 2‐acetolactic acid publication-title: Arch Biochem – ident: e_1_2_1_9_1 doi: 10.1016/S0167-4838(98)00083-1 – ident: e_1_2_1_3_1 doi: 10.1021/bi0104524 – ident: e_1_2_1_7_1 doi: 10.1111/j.1432-1033.1995.650_b.x – ident: e_1_2_1_16_1 doi: 10.1016/S1381-1177(00)00029-1 – ident: e_1_2_1_26_1 doi: 10.1016/S0076-6879(00)24222-5 – ident: e_1_2_1_4_1 doi: 10.1039/p19960000425 – ident: e_1_2_1_11_1 doi: 10.1039/p19900001367 – ident: e_1_2_1_23_1 doi: 10.1023/A:1008903817990 – ident: e_1_2_1_5_1 doi: 10.1016/0003-2697(76)90527-3 – ident: e_1_2_1_2_1 – ident: e_1_2_1_22_1 doi: 10.1016/S0167-4838(98)00071-5 – start-page: 352 year: 1987 ident: e_1_2_1_25_1 – ident: e_1_2_1_27_1 doi: 10.1016/S0958-1669(00)00139-7 – ident: e_1_2_1_24_1 doi: 10.1055/s-1977-24413 – ident: e_1_2_1_13_1 doi: 10.1007/BF00632526 – ident: e_1_2_1_19_1 doi: 10.1007/BFb0103301 – ident: e_1_2_1_8_1 doi: 10.1016/S0040-4039(00)80529-8 – start-page: 199 volume-title: Biosynthesis of branched chain amino acids year: 1990 ident: e_1_2_1_10_1 |
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| Snippet | We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of... We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of ( R... We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (> or =98% enantiomeric excess) synthesis of... We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (=>98% enantiomeric excess) synthesis of (R)-... |
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| SubjectTerms | acetolactate synthase Acetolactate Synthase - metabolism Acetone - analogs & derivatives Acetone - chemical synthesis Acetone - chemistry Acetone - isolation & purification benzaldehyde Benzaldehydes Binding Sites biocatalysis Biological and medical sciences Biotechnology Catalysis chiral enantiomeric excess Enzyme engineering Escherichia coli - enzymology Escherichia coli - genetics Fermentation Fundamental and applied biological sciences. Psychology hydroxyketone Isoenzymes - metabolism Methods. Procedures. Technologies Miscellaneous Molecular Structure pyruvate pyruvate decarboxylase Pyruvic Acid Stereoisomerism stereospecificity Temperature thiamin diphosphate Time Factors |
| Title | Acetohydroxyacid synthase: A new enzyme for chiral synthesis of R-phenylacetylcarbinol |
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