Recent structural insights into the expanding world of carbohydrate-active enzymes

G J  Davies; T M  Gloster; B  Henrissat

doi:10.1016/j.sbi.2005.10.008

Recent structural insights into the expanding world of carbohydrate-active enzymes

G J Davies, T M Gloster, B Henrissat

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Enzymes that catalyse the synthesis and breakdown of glycosidic bonds account for 1-3% of the proteins encoded by the genomes of most organisms. At the current rate, over 12 000 glycosyltransferase and glycoside hydrolase open reading frames will appear during 2006. Recent advances in the study of the structure and mechanism of these carbohydrate-active enzymes reveal that glycoside hydrolases continue to display a wide variety of scaffolds, whereas nucleotide-sugar-dependent glycosyltransferases tend to be grafted onto just two protein folds. The past two years have seen significant advances, including the discovery of a novel NAD(+)-dependent glycosidase mechanism, the dissection of the reaction coordinate of sialidases and a better understanding of the expanding roles of auxiliary carbohydrate-binding domains.

Original language	English
Pages (from-to)	637-645
Number of pages	9
Journal	CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume	15
Issue number	6
DOIs	https://doi.org/10.1016/j.sbi.2005.10.008
Publication status	Published - Dec 2005

Keywords

CRUZI TRANS-SIALIDASE
CRYSTAL-STRUCTURE
BACILLUS-SUBTILIS
THERMOTOGA-MARITIMA
3-DIMENSIONAL STRUCTURE
CATALYTIC MECHANISM
GLYCOSIDASE MECHANISMS
ANGSTROM RESOLUTION
BINDING-PROPERTIES
ALPHA-GLUCOSIDASE

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10.1016/j.sbi.2005.10.008

Cite this

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title = "Recent structural insights into the expanding world of carbohydrate-active enzymes",

abstract = "Enzymes that catalyse the synthesis and breakdown of glycosidic bonds account for 1-3% of the proteins encoded by the genomes of most organisms. At the current rate, over 12 000 glycosyltransferase and glycoside hydrolase open reading frames will appear during 2006. Recent advances in the study of the structure and mechanism of these carbohydrate-active enzymes reveal that glycoside hydrolases continue to display a wide variety of scaffolds, whereas nucleotide-sugar-dependent glycosyltransferases tend to be grafted onto just two protein folds. The past two years have seen significant advances, including the discovery of a novel NAD(+)-dependent glycosidase mechanism, the dissection of the reaction coordinate of sialidases and a better understanding of the expanding roles of auxiliary carbohydrate-binding domains.",

keywords = "CRUZI TRANS-SIALIDASE, CRYSTAL-STRUCTURE, BACILLUS-SUBTILIS, THERMOTOGA-MARITIMA, 3-DIMENSIONAL STRUCTURE, CATALYTIC MECHANISM, GLYCOSIDASE MECHANISMS, ANGSTROM RESOLUTION, BINDING-PROPERTIES, ALPHA-GLUCOSIDASE",

author = "Davies, {G J} and Gloster, {T M} and B Henrissat",

year = "2005",

month = dec,

doi = "10.1016/j.sbi.2005.10.008",

language = "English",

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pages = "637--645",

journal = "CURRENT OPINION IN STRUCTURAL BIOLOGY",

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publisher = "Elsevier",

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TY - JOUR

T1 - Recent structural insights into the expanding world of carbohydrate-active enzymes

AU - Davies, G J

AU - Gloster, T M

AU - Henrissat, B

PY - 2005/12

Y1 - 2005/12

N2 - Enzymes that catalyse the synthesis and breakdown of glycosidic bonds account for 1-3% of the proteins encoded by the genomes of most organisms. At the current rate, over 12 000 glycosyltransferase and glycoside hydrolase open reading frames will appear during 2006. Recent advances in the study of the structure and mechanism of these carbohydrate-active enzymes reveal that glycoside hydrolases continue to display a wide variety of scaffolds, whereas nucleotide-sugar-dependent glycosyltransferases tend to be grafted onto just two protein folds. The past two years have seen significant advances, including the discovery of a novel NAD(+)-dependent glycosidase mechanism, the dissection of the reaction coordinate of sialidases and a better understanding of the expanding roles of auxiliary carbohydrate-binding domains.

AB - Enzymes that catalyse the synthesis and breakdown of glycosidic bonds account for 1-3% of the proteins encoded by the genomes of most organisms. At the current rate, over 12 000 glycosyltransferase and glycoside hydrolase open reading frames will appear during 2006. Recent advances in the study of the structure and mechanism of these carbohydrate-active enzymes reveal that glycoside hydrolases continue to display a wide variety of scaffolds, whereas nucleotide-sugar-dependent glycosyltransferases tend to be grafted onto just two protein folds. The past two years have seen significant advances, including the discovery of a novel NAD(+)-dependent glycosidase mechanism, the dissection of the reaction coordinate of sialidases and a better understanding of the expanding roles of auxiliary carbohydrate-binding domains.

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KW - CRYSTAL-STRUCTURE

KW - BACILLUS-SUBTILIS

KW - THERMOTOGA-MARITIMA

KW - 3-DIMENSIONAL STRUCTURE

KW - CATALYTIC MECHANISM

KW - GLYCOSIDASE MECHANISMS

KW - ANGSTROM RESOLUTION

KW - BINDING-PROPERTIES

KW - ALPHA-GLUCOSIDASE

U2 - 10.1016/j.sbi.2005.10.008

DO - 10.1016/j.sbi.2005.10.008

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JO - CURRENT OPINION IN STRUCTURAL BIOLOGY

JF - CURRENT OPINION IN STRUCTURAL BIOLOGY

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ER -