InforLorV4, PascalFrancis, Corpus, bibRecord, 000269

A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B

Identifieur interne : 000269 ( PascalFrancis/Corpus ); précédent : 000268; suivant : 000270

A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B

Auteurs : Eduardo B. De Oliveira ; Catherine Humeau ; Latifa Chebil ; Elaine R. Maia ; François Dehez ; Bernard Maigret ; Mohamed Ghoul ; Jean-Marc Engasser

Source :

Journal of molecular catalysis. B, Enzymatic [ 1381-1177 ] ; 2009.

RBID : Pascal:09-0239458

Descripteurs français

Pascal (Inist)
- Modélisation, Régiosélectivité, Acylation, Flavonoïde, Glycoside, Candida antarctica, Catalyse, Triacylglycerol lipase.

English descriptors

KwdEn :
- Acylation, Catalysis, Flavonoid, Glycoside, Modeling, Regioselectivity, Triacylglycerol lipase, candida antarctica.

Abstract

The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 1381-1177`
A03		`1`		`@0 J. mol. catal., B Enzym.`
A05				`@2 59`
A06				`@2 1-3`
A08	`01`	`1`	`ENG`	`@1 A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B`
A11	`01`	`1`		`@1 DE OLIVEIRA (Eduardo B.)`
A11	`02`	`1`		`@1 HUMEAU (Catherine)`
A11	`03`	`1`		`@1 CHEBIL (Latifa)`
A11	`04`	`1`		`@1 MAIA (Elaine R.)`
A11	`05`	`1`		`@1 DEHEZ (François)`
A11	`06`	`1`		`@1 MAIGRET (Bernard)`
A11	`07`	`1`		`@1 GHOUL (Mohamed)`
A11	`08`	`1`		`@1 ENGASSER (Jean-Marc)`
A14	`01`			`@1 Laboratoire Biocatalyse Bioprocédés (LBB), ENSAIA-INPL, Nancy Université, 2 av. de la Forêt d'Haye @2 54500, Vandoeuvre-lès-Nancy @3 FRA @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 7 aut. @Z 8 aut.`
A14	`02`			`@1 Laboratorio de Estudos Estruturais Moleculares (LEEM), Instituto de Quimica, Universidade de Brasilia, CP 4478 @2 70904-970, Brasília-DF @3 BRA @Z 4 aut.`
A14	`03`			`@1 Equipe de Dynamique des Assemblages Membranaires (EDAM), CNRS, Université Henri Poincaré, 7565 @2 54500, Vandoeuvre-lès-Nancy @3 FRA @Z 5 aut.`
A14	`04`			`@1 Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA), CNRS, Université Henri Poincaré, BP 239 @2 54506, Vandoeuvre-lès-Nancy @3 FRA @Z 6 aut.`
A20				`@1 96-105`
A21				`@1 2009`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 17107B @5 354000187869970130`
A44				`@0 0000 @1 © 2009 INIST-CNRS. All rights reserved.`
A45				`@0 48 ref.`
A47	`01`	`1`		`@0 09-0239458`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Journal of molecular catalysis. B, Enzymatic`
A66	`01`			`@0 NLD`
C01	`01`		`ENG`	@0 The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.
C02	`01`	`X`		`@0 002A31C06`
C02	`02`	`X`		`@0 215`
C03	`01`	`X`	`FRE`	`@0 Modélisation @5 01`
C03	`01`	`X`	`ENG`	`@0 Modeling @5 01`
C03	`01`	`X`	`SPA`	`@0 Modelización @5 01`
C03	`02`	`X`	`FRE`	`@0 Régiosélectivité @5 02`
C03	`02`	`X`	`ENG`	`@0 Regioselectivity @5 02`
C03	`02`	`X`	`SPA`	`@0 Regioselectividad @5 02`
C03	`03`	`X`	`FRE`	`@0 Acylation @5 10`
C03	`03`	`X`	`ENG`	`@0 Acylation @5 10`
C03	`03`	`X`	`SPA`	`@0 Acilación @5 10`
C03	`04`	`X`	`FRE`	`@0 Flavonoïde @5 11`
C03	`04`	`X`	`ENG`	`@0 Flavonoid @5 11`
C03	`04`	`X`	`SPA`	`@0 Flavonoide @5 11`
C03	`05`	`X`	`FRE`	`@0 Glycoside @5 12`
C03	`05`	`X`	`ENG`	`@0 Glycoside @5 12`
C03	`05`	`X`	`SPA`	`@0 Glicósido @5 12`
C03	`06`	`X`	`FRE`	`@0 Candida antarctica @2 NS @5 13`
C03	`06`	`X`	`ENG`	`@0 candida antarctica @2 NS @5 13`
C03	`06`	`X`	`SPA`	`@0 candida antarctica @2 NS @5 13`
C03	`07`	`X`	`FRE`	`@0 Catalyse @5 19`
C03	`07`	`X`	`ENG`	`@0 Catalysis @5 19`
C03	`07`	`X`	`SPA`	`@0 Catálisis @5 19`
C03	`08`	`X`	`FRE`	`@0 Triacylglycerol lipase @2 FE @5 20`
C03	`08`	`X`	`ENG`	`@0 Triacylglycerol lipase @2 FE @5 20`
C03	`08`	`X`	`SPA`	`@0 Triacylglycerol lipase @2 FE @5 20`
C07	`01`	`X`	`FRE`	`@0 Fungi Imperfecti @2 NS`
C07	`01`	`X`	`ENG`	`@0 Fungi Imperfecti @2 NS`
C07	`01`	`X`	`SPA`	`@0 Fungi Imperfecti @2 NS`
C07	`02`	`X`	`FRE`	`@0 Fungi @2 NS`
C07	`02`	`X`	`ENG`	`@0 Fungi @2 NS`
C07	`02`	`X`	`SPA`	`@0 Fungi @2 NS`
C07	`03`	`X`	`FRE`	`@0 Carboxylic ester hydrolases @2 FE`
C07	`03`	`X`	`ENG`	`@0 Carboxylic ester hydrolases @2 FE`
C07	`03`	`X`	`SPA`	`@0 Carboxylic ester hydrolases @2 FE`
C07	`04`	`X`	`FRE`	`@0 Esterases @2 FE`
C07	`04`	`X`	`ENG`	`@0 Esterases @2 FE`
C07	`04`	`X`	`SPA`	`@0 Esterases @2 FE`
C07	`05`	`X`	`FRE`	`@0 Hydrolases @2 FE`
C07	`05`	`X`	`ENG`	`@0 Hydrolases @2 FE`
C07	`05`	`X`	`SPA`	`@0 Hydrolases @2 FE`
C07	`06`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`06`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`06`	`X`	`SPA`	`@0 Enzima @2 FE`
N21				`@1 173`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 09-0239458 INIST
ET :	A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B
AU :	DE OLIVEIRA (Eduardo B.); HUMEAU (Catherine); CHEBIL (Latifa); MAIA (Elaine R.); DEHEZ (François); MAIGRET (Bernard); GHOUL (Mohamed); ENGASSER (Jean-Marc)
AF :	Laboratoire Biocatalyse Bioprocédés (LBB), ENSAIA-INPL, Nancy Université, 2 av. de la Forêt d'Haye/54500, Vandoeuvre-lès-Nancy/France (1 aut., 2 aut., 3 aut., 7 aut., 8 aut.); Laboratorio de Estudos Estruturais Moleculares (LEEM), Instituto de Quimica, Universidade de Brasilia, CP 4478/70904-970, Brasília-DF/Brésil (4 aut.); Equipe de Dynamique des Assemblages Membranaires (EDAM), CNRS, Université Henri Poincaré, 7565/54500, Vandoeuvre-lès-Nancy/France (5 aut.); Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA), CNRS, Université Henri Poincaré, BP 239/54506, Vandoeuvre-lès-Nancy/France (6 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of molecular catalysis. B, Enzymatic; ISSN 1381-1177; Pays-Bas; Da. 2009; Vol. 59; No. 1-3; Pp. 96-105; Bibl. 48 ref.
LA :	Anglais
EA :	The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.
CC :	002A31C06; 215
FD :	Modélisation; Régiosélectivité; Acylation; Flavonoïde; Glycoside; Candida antarctica; Catalyse; Triacylglycerol lipase
FG :	Fungi Imperfecti; Fungi; Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme
ED :	Modeling; Regioselectivity; Acylation; Flavonoid; Glycoside; candida antarctica; Catalysis; Triacylglycerol lipase
EG :	Fungi Imperfecti; Fungi; Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme
SD :	Modelización; Regioselectividad; Acilación; Flavonoide; Glicósido; candida antarctica; Catálisis; Triacylglycerol lipase
LO :	INIST-17107B.354000187869970130
ID :	09-0239458

Links to Exploration step

Pascal:09-0239458

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acylation</term>
<term>Catalysis</term>
<term>Flavonoid</term>
<term>Glycoside</term>
<term>Modeling</term>
<term>Regioselectivity</term>
<term>Triacylglycerol lipase</term>
<term>candida antarctica</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Modélisation</term>
<term>Régiosélectivité</term>
<term>Acylation</term>
<term>Flavonoïde</term>
<term>Glycoside</term>
<term>Candida antarctica</term>
<term>Catalyse</term>
<term>Triacylglycerol lipase</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.</div>
</front>
</TEI>
<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>1381-1177</s0>
</fA01>
<fA03 i2="1"><s0>J. mol. catal., B Enzym.</s0>
</fA03>
<fA05><s2>59</s2>
</fA05>
<fA06><s2>1-3</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>DE OLIVEIRA (Eduardo B.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>HUMEAU (Catherine)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>CHEBIL (Latifa)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>MAIA (Elaine R.)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>DEHEZ (François)</s1>
</fA11>
<fA11 i1="06" i2="1"><s1>MAIGRET (Bernard)</s1>
</fA11>
<fA11 i1="07" i2="1"><s1>GHOUL (Mohamed)</s1>
</fA11>
<fA11 i1="08" i2="1"><s1>ENGASSER (Jean-Marc)</s1>
</fA11>
<fA14 i1="01"><s1>Laboratoire Biocatalyse Bioprocédés (LBB), ENSAIA-INPL, Nancy Université, 2 av. de la Forêt d'Haye</s1>
<s2>54500, Vandoeuvre-lès-Nancy</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Laboratorio de Estudos Estruturais Moleculares (LEEM), Instituto de Quimica, Universidade de Brasilia, CP 4478</s1>
<s2>70904-970, Brasília-DF</s2>
<s3>BRA</s3>
<sZ>4 aut.</sZ>
</fA14>
<fA14 i1="03"><s1>Equipe de Dynamique des Assemblages Membranaires (EDAM), CNRS, Université Henri Poincaré, 7565</s1>
<s2>54500, Vandoeuvre-lès-Nancy</s2>
<s3>FRA</s3>
<sZ>5 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA), CNRS, Université Henri Poincaré, BP 239</s1>
<s2>54506, Vandoeuvre-lès-Nancy</s2>
<s3>FRA</s3>
<sZ>6 aut.</sZ>
</fA14>
<fA20><s1>96-105</s1>
</fA20>
<fA21><s1>2009</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>17107B</s2>
<s5>354000187869970130</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2009 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>48 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>09-0239458</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Journal of molecular catalysis. B, Enzymatic</s0>
</fA64>
<fA66 i1="01"><s0>NLD</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A31C06</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>215</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Modélisation</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Modeling</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Modelización</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Régiosélectivité</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Regioselectivity</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Regioselectividad</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Acylation</s0>
<s5>10</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Acylation</s0>
<s5>10</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Acilación</s0>
<s5>10</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Flavonoïde</s0>
<s5>11</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Flavonoid</s0>
<s5>11</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Flavonoide</s0>
<s5>11</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Glycoside</s0>
<s5>12</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Glycoside</s0>
<s5>12</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Glicósido</s0>
<s5>12</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Candida antarctica</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>candida antarctica</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>candida antarctica</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Catalyse</s0>
<s5>19</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Catalysis</s0>
<s5>19</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Catálisis</s0>
<s5>19</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Triacylglycerol lipase</s0>
<s2>FE</s2>
<s5>20</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Triacylglycerol lipase</s0>
<s2>FE</s2>
<s5>20</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Triacylglycerol lipase</s0>
<s2>FE</s2>
<s5>20</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Fungi Imperfecti</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Fungi Imperfecti</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Fungi Imperfecti</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Fungi</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Fungi</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Fungi</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Carboxylic ester hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Carboxylic ester hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Carboxylic ester hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Esterases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Esterases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Esterases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>173</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 09-0239458 INIST</NO>
<ET>A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B</ET>
<AU>DE OLIVEIRA (Eduardo B.); HUMEAU (Catherine); CHEBIL (Latifa); MAIA (Elaine R.); DEHEZ (François); MAIGRET (Bernard); GHOUL (Mohamed); ENGASSER (Jean-Marc)</AU>
<AF>Laboratoire Biocatalyse Bioprocédés (LBB), ENSAIA-INPL, Nancy Université, 2 av. de la Forêt d'Haye/54500, Vandoeuvre-lès-Nancy/France (1 aut., 2 aut., 3 aut., 7 aut., 8 aut.); Laboratorio de Estudos Estruturais Moleculares (LEEM), Instituto de Quimica, Universidade de Brasilia, CP 4478/70904-970, Brasília-DF/Brésil (4 aut.); Equipe de Dynamique des Assemblages Membranaires (EDAM), CNRS, Université Henri Poincaré, 7565/54500, Vandoeuvre-lès-Nancy/France (5 aut.); Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA), CNRS, Université Henri Poincaré, BP 239/54506, Vandoeuvre-lès-Nancy/France (6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of molecular catalysis. B, Enzymatic; ISSN 1381-1177; Pays-Bas; Da. 2009; Vol. 59; No. 1-3; Pp. 96-105; Bibl. 48 ref.</SO>
<LA>Anglais</LA>
<EA>The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion ; (2) stability of hydrogen bond interactions with the oxyanion hole residues: (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoids was placed close to the pocket bottom. In particular, only the primary 6"-OH of the isoquercitrin glucose and the secondary 4"'-OH of the rutin rhamnose were expected to be acetylated, as they were the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation.</EA>
<CC>002A31C06; 215</CC>
<FD>Modélisation; Régiosélectivité; Acylation; Flavonoïde; Glycoside; Candida antarctica; Catalyse; Triacylglycerol lipase</FD>
<FG>Fungi Imperfecti; Fungi; Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme</FG>
<ED>Modeling; Regioselectivity; Acylation; Flavonoid; Glycoside; candida antarctica; Catalysis; Triacylglycerol lipase</ED>
<EG>Fungi Imperfecti; Fungi; Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme</EG>
<SD>Modelización; Regioselectividad; Acilación; Flavonoide; Glicósido; candida antarctica; Catálisis; Triacylglycerol lipase</SD>
<LO>INIST-17107B.354000187869970130</LO>
<ID>09-0239458</ID>
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A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B

A molecular modelling study to rationalize the regioselectivity in acylation of flavonoid glycosides catalyzed by Candida antarctica lipase B

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