Publication

The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes

Gangoiti, J., Pijning, T. & Dijkhuizen, L., 20-Nov-2015, In : Applied and environmental microbiology. 82, 2, p. 756-766 11 p., AEM.03420-15.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Gangoiti, J., Pijning, T., & Dijkhuizen, L. (2015). The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Applied and environmental microbiology, 82(2), 756-766. [AEM.03420-15]. https://doi.org/10.1128/AEM.03420-15

Author

Gangoiti, Joana ; Pijning, Tjaard ; Dijkhuizen, Lubbert. / The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. In: Applied and environmental microbiology. 2015 ; Vol. 82, No. 2. pp. 756-766.

Harvard

Gangoiti, J, Pijning, T & Dijkhuizen, L 2015, 'The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes', Applied and environmental microbiology, vol. 82, no. 2, AEM.03420-15, pp. 756-766. https://doi.org/10.1128/AEM.03420-15

Standard

The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. / Gangoiti, Joana; Pijning, Tjaard; Dijkhuizen, Lubbert.

In: Applied and environmental microbiology, Vol. 82, No. 2, AEM.03420-15, 20.11.2015, p. 756-766.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Gangoiti J, Pijning T, Dijkhuizen L. The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Applied and environmental microbiology. 2015 Nov 20;82(2):756-766. AEM.03420-15. https://doi.org/10.1128/AEM.03420-15


BibTeX

@article{52bb8e9489504fa1841a9266d50e3294,
title = "The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes",
abstract = "The Glycoside Hydrolase (GH) family 70 originally was established for glucansucrase enzymes, solely found in lactic acid bacteria, synthesizing α-glucan polysaccharides from sucrose (e.g. GtfA). In recent years we have characterized GtfB and related Lactobacillus enzymes as 4,6-α-glucanotransferase enzymes. These GtfB type of enzymes constitute a first GH70 subfamily, unable to act on sucrose as substrate, but active with maltodextrins and starch, cleaving (α1→4) linkages and synthesizing linear (α1→6)-glucan chains. The GtfB disproportionating type of activity results in conversion of malto-oligosaccharides into IsoMalto-/Malto-Polysaccharides with a relatively high percentage of (α1→6) linkages.This paper reports the identification of a second GH70 subfamily (designated GtfC enzymes) and the characterization of the Exiguobacterium sibiricum 255-15 GtfC enzyme, also inactive with sucrose and displaying 4,6-α-glucanotransferase activity with malto-oligosaccharides. GtfC differs from GtfB in synthesizing IsoMalto-/Malto-Oligosaccharides. Biochemically the GtfB and GtfC type of enzymes are related but phylogenetically they clearly constitute different GH70 subfamilies, displaying only 30% sequence identity. Whereas GtfB type of enzymes largely have the same domain order as glucansucrases (with α-amylase domains A, B, C, plus domains IV and V), this GtfC type of enzyme differs in the order of these domains and completely lacks domain V. In GtfC the sequence of the conserved regions I-IV of clan GH-H is identical to that in GH13 (I-II-III-IV) but different from that in GH70 (II-III-IV-I due to a circular permutation of the (β/α)8-barrel). The GtfC 4,6-α-glucanotransferase enzymes thus represent structurally and functionally very interesting evolutionary intermediates between α-amylase and glucansucrase enzymes.",
author = "Joana Gangoiti and Tjaard Pijning and Lubbert Dijkhuizen",
note = "Copyright {\textcopyright} 2015, American Society for Microbiology. All Rights Reserved.",
year = "2015",
month = nov,
day = "20",
doi = "10.1128/AEM.03420-15",
language = "English",
volume = "82",
pages = "756--766",
journal = "Applied Environmental Microbiology",
issn = "0099-2240",
publisher = "AMER SOC MICROBIOLOGY",
number = "2",

}

RIS

TY - JOUR

T1 - The Exiguobacterium sibiricum 255-15 GtfC enzyme representing a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes

AU - Gangoiti, Joana

AU - Pijning, Tjaard

AU - Dijkhuizen, Lubbert

N1 - Copyright © 2015, American Society for Microbiology. All Rights Reserved.

PY - 2015/11/20

Y1 - 2015/11/20

N2 - The Glycoside Hydrolase (GH) family 70 originally was established for glucansucrase enzymes, solely found in lactic acid bacteria, synthesizing α-glucan polysaccharides from sucrose (e.g. GtfA). In recent years we have characterized GtfB and related Lactobacillus enzymes as 4,6-α-glucanotransferase enzymes. These GtfB type of enzymes constitute a first GH70 subfamily, unable to act on sucrose as substrate, but active with maltodextrins and starch, cleaving (α1→4) linkages and synthesizing linear (α1→6)-glucan chains. The GtfB disproportionating type of activity results in conversion of malto-oligosaccharides into IsoMalto-/Malto-Polysaccharides with a relatively high percentage of (α1→6) linkages.This paper reports the identification of a second GH70 subfamily (designated GtfC enzymes) and the characterization of the Exiguobacterium sibiricum 255-15 GtfC enzyme, also inactive with sucrose and displaying 4,6-α-glucanotransferase activity with malto-oligosaccharides. GtfC differs from GtfB in synthesizing IsoMalto-/Malto-Oligosaccharides. Biochemically the GtfB and GtfC type of enzymes are related but phylogenetically they clearly constitute different GH70 subfamilies, displaying only 30% sequence identity. Whereas GtfB type of enzymes largely have the same domain order as glucansucrases (with α-amylase domains A, B, C, plus domains IV and V), this GtfC type of enzyme differs in the order of these domains and completely lacks domain V. In GtfC the sequence of the conserved regions I-IV of clan GH-H is identical to that in GH13 (I-II-III-IV) but different from that in GH70 (II-III-IV-I due to a circular permutation of the (β/α)8-barrel). The GtfC 4,6-α-glucanotransferase enzymes thus represent structurally and functionally very interesting evolutionary intermediates between α-amylase and glucansucrase enzymes.

AB - The Glycoside Hydrolase (GH) family 70 originally was established for glucansucrase enzymes, solely found in lactic acid bacteria, synthesizing α-glucan polysaccharides from sucrose (e.g. GtfA). In recent years we have characterized GtfB and related Lactobacillus enzymes as 4,6-α-glucanotransferase enzymes. These GtfB type of enzymes constitute a first GH70 subfamily, unable to act on sucrose as substrate, but active with maltodextrins and starch, cleaving (α1→4) linkages and synthesizing linear (α1→6)-glucan chains. The GtfB disproportionating type of activity results in conversion of malto-oligosaccharides into IsoMalto-/Malto-Polysaccharides with a relatively high percentage of (α1→6) linkages.This paper reports the identification of a second GH70 subfamily (designated GtfC enzymes) and the characterization of the Exiguobacterium sibiricum 255-15 GtfC enzyme, also inactive with sucrose and displaying 4,6-α-glucanotransferase activity with malto-oligosaccharides. GtfC differs from GtfB in synthesizing IsoMalto-/Malto-Oligosaccharides. Biochemically the GtfB and GtfC type of enzymes are related but phylogenetically they clearly constitute different GH70 subfamilies, displaying only 30% sequence identity. Whereas GtfB type of enzymes largely have the same domain order as glucansucrases (with α-amylase domains A, B, C, plus domains IV and V), this GtfC type of enzyme differs in the order of these domains and completely lacks domain V. In GtfC the sequence of the conserved regions I-IV of clan GH-H is identical to that in GH13 (I-II-III-IV) but different from that in GH70 (II-III-IV-I due to a circular permutation of the (β/α)8-barrel). The GtfC 4,6-α-glucanotransferase enzymes thus represent structurally and functionally very interesting evolutionary intermediates between α-amylase and glucansucrase enzymes.

U2 - 10.1128/AEM.03420-15

DO - 10.1128/AEM.03420-15

M3 - Article

C2 - 26590275

VL - 82

SP - 756

EP - 766

JO - Applied Environmental Microbiology

JF - Applied Environmental Microbiology

SN - 0099-2240

IS - 2

M1 - AEM.03420-15

ER -

ID: 26258868