Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin

Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate... Plant Molecular Biology 37: 1–13, 1998. 1 c 1998 Kluwer Academic Publishers. Printed in Belgium. Review Article Plant -glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin Torben P. Frandsen and Birte Svensson Carlsberg Laboratory, Department of Chemistry, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark ( author for correspondence) Received 2 December 1997; accepted 8 December 1997 Key words: retaining mechanism, sequence similarity, mechanism-based labelling, catalytic residues, multiple molecular forms, starch degradation Abbreviations: G2, maltose; iG2, isomaltose; G3, maltotriose; G4, maltotetraose; G5, maltopentaose; G6, malto- hexaose; G7, maltoheptaose; G8, maltooctaose; pNPG, p-nitrophenyl -D-glucopyranoside Introduction Glycoside hydrolases are currently classified into more than 60 families [22, 23]; -glucosidases belong -Glucosidases (EC 3.2.1.20, -D-glucoside gluc- to families 13 and 31 [22, 23] based on their amino acid ohydrolase) constitute a group of exo-acting glycos- sequence. This provides information on the structure ide hydrolases of diverse specificity that catalyze the of the catalytic site as well as, for several enzymes, release of -D-glucose from the non-reducing end of - the three-dimensional fold [14]. Glycoside hydro- linked substrates. Oligo-1,6-glucosidase (EC 3.2.1.10) lase family 31 currently contains -glucosidases from and sucrase-isomaltase http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin

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Publisher
Springer Journals
Copyright
Copyright © 1998 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005925819741
Publisher site
See Article on Publisher Site

Abstract

Plant Molecular Biology 37: 1–13, 1998. 1 c 1998 Kluwer Academic Publishers. Printed in Belgium. Review Article Plant -glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin Torben P. Frandsen and Birte Svensson Carlsberg Laboratory, Department of Chemistry, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark ( author for correspondence) Received 2 December 1997; accepted 8 December 1997 Key words: retaining mechanism, sequence similarity, mechanism-based labelling, catalytic residues, multiple molecular forms, starch degradation Abbreviations: G2, maltose; iG2, isomaltose; G3, maltotriose; G4, maltotetraose; G5, maltopentaose; G6, malto- hexaose; G7, maltoheptaose; G8, maltooctaose; pNPG, p-nitrophenyl -D-glucopyranoside Introduction Glycoside hydrolases are currently classified into more than 60 families [22, 23]; -glucosidases belong -Glucosidases (EC 3.2.1.20, -D-glucoside gluc- to families 13 and 31 [22, 23] based on their amino acid ohydrolase) constitute a group of exo-acting glycos- sequence. This provides information on the structure ide hydrolases of diverse specificity that catalyze the of the catalytic site as well as, for several enzymes, release of -D-glucose from the non-reducing end of - the three-dimensional fold [14]. Glycoside hydro- linked substrates. Oligo-1,6-glucosidase (EC 3.2.1.10) lase family 31 currently contains -glucosidases from and sucrase-isomaltase

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 6, 2004

References

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