Structure and function of α-glucan debranching enzymes

Forskningsoutput: TidskriftsbidragÖversiktsartikel

Standard

Structure and function of α-glucan debranching enzymes. / Møller, Marie Sofie; Henriksen, Anette; Svensson, Birte.

I: Cellular and Molecular Life Sciences, Vol. 73, Nr. 14, 01.07.2016, s. 2619-2641.

Forskningsoutput: TidskriftsbidragÖversiktsartikel

Harvard

APA

CBE

MLA

Vancouver

Author

Møller, Marie Sofie ; Henriksen, Anette ; Svensson, Birte. / Structure and function of α-glucan debranching enzymes. I: Cellular and Molecular Life Sciences. 2016 ; Vol. 73, Nr. 14. s. 2619-2641.

RIS

TY - JOUR

T1 - Structure and function of α-glucan debranching enzymes

AU - Møller, Marie Sofie

AU - Henriksen, Anette

AU - Svensson, Birte

PY - 2016/7/1

Y1 - 2016/7/1

N2 - α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central role in energy metabolism in all living organisms. They belong to glycoside hydrolase families GH13 and GH57 and several of these enzymes are industrially important. Nine GH13 subfamilies include α-glucan debranching enzymes; isoamylase and glycogen debranching enzymes (GH13_11); pullulanase type I/limit dextrinase (GH13_12–14); pullulan hydrolase (GH13_20); bifunctional glycogen debranching enzyme (GH13_25); oligo-1 and glucan-1,6-α-glucosidases (GH13_31); pullulanase type II (GH13_39); and α-amylase domains (GH13_41) in two-domain amylase–pullulanases. GH57 harbours type II pullulanases. Specificity differences, domain organisation, carbohydrate binding modules, sequence motifs, three-dimensional structures and specificity determinants are discussed. The phylogenetic analysis indicated that GH13_39 enzymes could represent a “missing link” between the strictly α-1,6-specific debranching enzymes and the enzymes with dual specificity and α-1,4-linkage preference.

AB - α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central role in energy metabolism in all living organisms. They belong to glycoside hydrolase families GH13 and GH57 and several of these enzymes are industrially important. Nine GH13 subfamilies include α-glucan debranching enzymes; isoamylase and glycogen debranching enzymes (GH13_11); pullulanase type I/limit dextrinase (GH13_12–14); pullulan hydrolase (GH13_20); bifunctional glycogen debranching enzyme (GH13_25); oligo-1 and glucan-1,6-α-glucosidases (GH13_31); pullulanase type II (GH13_39); and α-amylase domains (GH13_41) in two-domain amylase–pullulanases. GH57 harbours type II pullulanases. Specificity differences, domain organisation, carbohydrate binding modules, sequence motifs, three-dimensional structures and specificity determinants are discussed. The phylogenetic analysis indicated that GH13_39 enzymes could represent a “missing link” between the strictly α-1,6-specific debranching enzymes and the enzymes with dual specificity and α-1,4-linkage preference.

KW - Carbohydrate binding modules

KW - Domain architecture

KW - Glycoside hydrolase family 13 subfamilies

KW - Multi-domain three-dimensional structure

KW - Phylogeny

KW - Sequence motifs and determinants

KW - Structure–function relationship

KW - Substrate specificity

UR - http://www.scopus.com/inward/record.url?scp=84965052610&partnerID=8YFLogxK

U2 - 10.1007/s00018-016-2241-y

DO - 10.1007/s00018-016-2241-y

M3 - Review article

VL - 73

SP - 2619

EP - 2641

JO - Cellular and Molecular Life Sciences

T2 - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-9071

IS - 14

ER -