Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases

Antoni Planas; Carles Malet

doi:10.1016/S0921-0423(06)80096-1

Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases

Antoni Planas^*
, Carles Malet

^*Corresponding author for this work

IQS School of Engineering

Research output: Book chapter › Conference contribution › peer-review

9 Citations (Web of Science)

Abstract

Specific low molecular weight oligosaccharides having a chromophoric aglycon were synthesized for kinetic evaluation of the enzyme catalysis. A subsite mapping study showed that the active site cleft is composed of four subsites on the non-reducing end, and allowed to estimate the contribution of subsites-II—-IV to transition state stabilization. In addition to a proper orientation of the scissile glycosidic bond of the substrate, inhibition kinetics with β-glucan- and cello-oligosaccharides suggest a binding preference of subsite -I for a 3-O-substituted over a 4-O-substituted glucopyranose unit. Subsite +I, on the other hand, has a minor contribution to binding but the nature of the aglycon in the substrate largely affects catalysis.

Original language	English
Title of host publication	Carbohydrate Bioengineering
Editors	SB Petersen, B Svensson, S Pedersen
Publisher	Elsevier
Pages	85-95
Number of pages	10
Edition	C
ISBN (Print)	978-0-444-82223-9
DOIs	https://doi.org/10.1016/S0921-0423(06)80096-1
Publication status	Published - 1995
Event	International Conference on Carbohydrate Bioengineering - HELSINGOR, Denmark Duration: 23 Apr 1995 → 26 Apr 1995

Publication series

Name	Progress in Biotechnology
Volume	10
ISSN (Print)	0921-0423

Conference

Conference	International Conference on Carbohydrate Bioengineering
Country/Territory	Denmark
City	HELSINGOR
Period	23/04/95 → 26/04/95

Access to Document

10.1016/S0921-0423(06)80096-1

Cite this

@inproceedings{bcf56630981a4d0395bcbf2b95a661c9,

title = "Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases",

abstract = "Specific low molecular weight oligosaccharides having a chromophoric aglycon were synthesized for kinetic evaluation of the enzyme catalysis. A subsite mapping study showed that the active site cleft is composed of four subsites on the non-reducing end, and allowed to estimate the contribution of subsites-II—-IV to transition state stabilization. In addition to a proper orientation of the scissile glycosidic bond of the substrate, inhibition kinetics with β-glucan- and cello-oligosaccharides suggest a binding preference of subsite -I for a 3-O-substituted over a 4-O-substituted glucopyranose unit. Subsite +I, on the other hand, has a minor contribution to binding but the nature of the aglycon in the substrate largely affects catalysis.",

author = "Antoni Planas and Carles Malet",

year = "1995",

doi = "10.1016/S0921-0423(06)80096-1",

language = "English",

isbn = "978-0-444-82223-9",

series = "Progress in Biotechnology",

publisher = "Elsevier",

pages = "85--95",

editor = "SB Petersen and B Svensson and S Pedersen",

booktitle = "Carbohydrate Bioengineering",

address = "Netherlands",

edition = "C",

note = "International Conference on Carbohydrate Bioengineering ; Conference date: 23-04-1995 Through 26-04-1995",

}

Planas, A & Malet, C 1995, Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases. in SB Petersen, B Svensson & S Pedersen (eds), Carbohydrate Bioengineering. C edn, Progress in Biotechnology, vol. 10, Elsevier, pp. 85-95, International Conference on Carbohydrate Bioengineering, HELSINGOR, Denmark, 23/04/95. https://doi.org/10.1016/S0921-0423(06)80096-1

Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases. / Planas, Antoni ; Malet, Carles.
Carbohydrate Bioengineering. ed. / SB Petersen; B Svensson; S Pedersen. C. ed. Elsevier, 1995. p. 85-95 (Progress in Biotechnology; Vol. 10).

Research output: Book chapter › Conference contribution › peer-review

TY - GEN

T1 - Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases

AU - Planas, Antoni

AU - Malet, Carles

PY - 1995

Y1 - 1995

N2 - Specific low molecular weight oligosaccharides having a chromophoric aglycon were synthesized for kinetic evaluation of the enzyme catalysis. A subsite mapping study showed that the active site cleft is composed of four subsites on the non-reducing end, and allowed to estimate the contribution of subsites-II—-IV to transition state stabilization. In addition to a proper orientation of the scissile glycosidic bond of the substrate, inhibition kinetics with β-glucan- and cello-oligosaccharides suggest a binding preference of subsite -I for a 3-O-substituted over a 4-O-substituted glucopyranose unit. Subsite +I, on the other hand, has a minor contribution to binding but the nature of the aglycon in the substrate largely affects catalysis.

AB - Specific low molecular weight oligosaccharides having a chromophoric aglycon were synthesized for kinetic evaluation of the enzyme catalysis. A subsite mapping study showed that the active site cleft is composed of four subsites on the non-reducing end, and allowed to estimate the contribution of subsites-II—-IV to transition state stabilization. In addition to a proper orientation of the scissile glycosidic bond of the substrate, inhibition kinetics with β-glucan- and cello-oligosaccharides suggest a binding preference of subsite -I for a 3-O-substituted over a 4-O-substituted glucopyranose unit. Subsite +I, on the other hand, has a minor contribution to binding but the nature of the aglycon in the substrate largely affects catalysis.

UR - https://www.scopus.com/pages/publications/7344225024

UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=pure_univeritat_ramon_llull&SrcAuth=WosAPI&KeyUT=WOS:A1995BE87L00008&DestLinkType=FullRecord&DestApp=WOS

U2 - 10.1016/S0921-0423(06)80096-1

DO - 10.1016/S0921-0423(06)80096-1

M3 - Conference contribution

AN - SCOPUS:7344225024

SN - 978-0-444-82223-9

T3 - Progress in Biotechnology

SP - 85

EP - 95

BT - Carbohydrate Bioengineering

A2 - Petersen, SB

A2 - Svensson, B

A2 - Pedersen, S

PB - Elsevier

T2 - International Conference on Carbohydrate Bioengineering

Y2 - 23 April 1995 through 26 April 1995

ER -

Contribution of subsites to catalysis and specificity in the extended binding cleft of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases

Abstract

Publication series

Conference

Access to Document

Other files and links

Fingerprint

Cite this