Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus

Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characterist...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Honda, K. [verfasserIn] Kataoka, M. Shimizu, S.

Format:	Artikel
Sprache:	Englisch

Erschienen:	2002

Schlagwörter:	Enzyme Methyl Ester Escherichia Coli Hydrolysis

Anmerkung:	© Springer-Verlag 2002

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 60(2002), 3 vom: Nov., Seite 288-292
Übergeordnetes Werk:	volume:60 ; year:2002 ; number:3 ; month:11 ; pages:288-292

Links:	Volltext

DOI / URN:	10.1007/s00253-002-1116-3

Katalog-ID:	OLC2050695608

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245	1	0	\|a Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
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520			\|a Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently.
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allfields	10.1007/s00253-002-1116-3 doi (DE-627)OLC2050695608 (DE-He213)s00253-002-1116-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Honda, K. verfasserin aut Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2002 Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. Enzyme Methyl Ester Escherichia Coli Hydrolysis Kataoka, M. aut Shimizu, S. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 60(2002), 3 vom: Nov., Seite 288-292 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:60 year:2002 number:3 month:11 pages:288-292 https://doi.org/10.1007/s00253-002-1116-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 60 2002 3 11 288-292
spelling	10.1007/s00253-002-1116-3 doi (DE-627)OLC2050695608 (DE-He213)s00253-002-1116-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Honda, K. verfasserin aut Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2002 Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. Enzyme Methyl Ester Escherichia Coli Hydrolysis Kataoka, M. aut Shimizu, S. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 60(2002), 3 vom: Nov., Seite 288-292 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:60 year:2002 number:3 month:11 pages:288-292 https://doi.org/10.1007/s00253-002-1116-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 60 2002 3 11 288-292
allfields_unstemmed	10.1007/s00253-002-1116-3 doi (DE-627)OLC2050695608 (DE-He213)s00253-002-1116-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Honda, K. verfasserin aut Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2002 Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. Enzyme Methyl Ester Escherichia Coli Hydrolysis Kataoka, M. aut Shimizu, S. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 60(2002), 3 vom: Nov., Seite 288-292 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:60 year:2002 number:3 month:11 pages:288-292 https://doi.org/10.1007/s00253-002-1116-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 60 2002 3 11 288-292
allfieldsGer	10.1007/s00253-002-1116-3 doi (DE-627)OLC2050695608 (DE-He213)s00253-002-1116-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Honda, K. verfasserin aut Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2002 Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. Enzyme Methyl Ester Escherichia Coli Hydrolysis Kataoka, M. aut Shimizu, S. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 60(2002), 3 vom: Nov., Seite 288-292 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:60 year:2002 number:3 month:11 pages:288-292 https://doi.org/10.1007/s00253-002-1116-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 60 2002 3 11 288-292
allfieldsSound	10.1007/s00253-002-1116-3 doi (DE-627)OLC2050695608 (DE-He213)s00253-002-1116-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Honda, K. verfasserin aut Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2002 Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. Enzyme Methyl Ester Escherichia Coli Hydrolysis Kataoka, M. aut Shimizu, S. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 60(2002), 3 vom: Nov., Seite 288-292 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:60 year:2002 number:3 month:11 pages:288-292 https://doi.org/10.1007/s00253-002-1116-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 60 2002 3 11 288-292
language	English
source	Enthalten in Applied microbiology and biotechnology 60(2002), 3 vom: Nov., Seite 288-292 volume:60 year:2002 number:3 month:11 pages:288-292
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topic_facet	Enzyme Methyl Ester Escherichia Coli Hydrolysis
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author	Honda, K.
spellingShingle	Honda, K. ddc 570 ssgn 12 fid BIODIV misc Enzyme misc Methyl misc Ester misc Escherichia Coli misc Hydrolysis Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus Enzyme Methyl Ester Escherichia Coli Hydrolysis
topic	ddc 570 ssgn 12 fid BIODIV misc Enzyme misc Methyl misc Ester misc Escherichia Coli misc Hydrolysis
topic_unstemmed	ddc 570 ssgn 12 fid BIODIV misc Enzyme misc Methyl misc Ester misc Escherichia Coli misc Hydrolysis
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title	Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
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title_full	Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
author_sort	Honda, K.
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author_browse	Honda, K. Kataoka, M. Shimizu, S.
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title_sort	enzymatic preparation of d-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from acinetobacter calcoaceticus
title_auth	Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
abstract	Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. © Springer-Verlag 2002
abstractGer	Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. © Springer-Verlag 2002
abstract_unstemmed	Abstract. 3,4-Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus F46, which was previously found on screening for aromatic lactone-hydrolyzing enzymes, catalyzes the hydrolysis of several linear esters. The substrate specificity of the enzyme toward linear esters was quite characteristic, i.e., (1) it was specific toward methyl esters, (2) it recognized the configuration at the 2-position, and (3) it hydrolyzed diesters to monoesters. DCH hydrolyzed the methyl esters of β-acetylthioisobutyrate and cetraxate. The products of these reactions were identified as D-β-acetylthioisobutyrate and cetraxate, respectively, i.e., the hydrolysis reactions catalyzed by DCH were stereo- and/or regioselective. With recombinant Escherichia coli cells expressing the DCH gene as a catalyst, stereospecific hydrolysis of methyl β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate proceeded efficiently. © Springer-Verlag 2002
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container_issue	3
title_short	Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus
url	https://doi.org/10.1007/s00253-002-1116-3
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up_date	2024-07-04T02:36:37.623Z
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Enzymatic preparation of D-β-acetylthioisobutyric acid and cetraxate hydrochloride using a stereo- and/or regioselective hydrolase, 3,4-dihydrocoumarin hydrolase from Acinetobacter calcoaceticus

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