Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut

Darrell W. Cockburn, Carolyn Suh, Krizia Perez Medina, Rebecca M. Duvall, Zdzislaw Wawrzak, Bernard Henrissat, Nicole M. Koropatkin*

*Corresponding author for this work

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here, we demonstrate that the cell wall anchored starch-degrading α-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme toward corn starches by ∼40-fold, down to the level of activity toward potato starch, suggesting that the CBMs facilitate activity on corn starch and allow its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms.

Original languageEnglish (US)
Pages (from-to)249-264
Number of pages16
JournalMolecular Microbiology
Volume107
Issue number2
DOIs
StatePublished - Jan 1 2018

Fingerprint

Eubacterium
Amylases
Starch
Carbohydrates
Zea mays
Solanum tuberosum
Bacteria
Amylose
Butyrates
Glycoside Hydrolases
Cell Wall

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Cockburn, Darrell W. ; Suh, Carolyn ; Medina, Krizia Perez ; Duvall, Rebecca M. ; Wawrzak, Zdzislaw ; Henrissat, Bernard ; Koropatkin, Nicole M. / Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut. In: Molecular Microbiology. 2018 ; Vol. 107, No. 2. pp. 249-264.
@article{bb88cc37140c4e9b8053c566df072f33,
title = "Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut",
abstract = "Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here, we demonstrate that the cell wall anchored starch-degrading α-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme toward corn starches by ∼40-fold, down to the level of activity toward potato starch, suggesting that the CBMs facilitate activity on corn starch and allow its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms.",
author = "Cockburn, {Darrell W.} and Carolyn Suh and Medina, {Krizia Perez} and Duvall, {Rebecca M.} and Zdzislaw Wawrzak and Bernard Henrissat and Koropatkin, {Nicole M.}",
year = "2018",
month = "1",
day = "1",
doi = "10.1111/mmi.13881",
language = "English (US)",
volume = "107",
pages = "249--264",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "2",

}

Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut. / Cockburn, Darrell W.; Suh, Carolyn; Medina, Krizia Perez; Duvall, Rebecca M.; Wawrzak, Zdzislaw; Henrissat, Bernard; Koropatkin, Nicole M.

In: Molecular Microbiology, Vol. 107, No. 2, 01.01.2018, p. 249-264.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut

AU - Cockburn, Darrell W.

AU - Suh, Carolyn

AU - Medina, Krizia Perez

AU - Duvall, Rebecca M.

AU - Wawrzak, Zdzislaw

AU - Henrissat, Bernard

AU - Koropatkin, Nicole M.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here, we demonstrate that the cell wall anchored starch-degrading α-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme toward corn starches by ∼40-fold, down to the level of activity toward potato starch, suggesting that the CBMs facilitate activity on corn starch and allow its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms.

AB - Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here, we demonstrate that the cell wall anchored starch-degrading α-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme toward corn starches by ∼40-fold, down to the level of activity toward potato starch, suggesting that the CBMs facilitate activity on corn starch and allow its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms.

UR - http://www.scopus.com/inward/record.url?scp=85036546359&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85036546359&partnerID=8YFLogxK

U2 - 10.1111/mmi.13881

DO - 10.1111/mmi.13881

M3 - Article

C2 - 29139580

AN - SCOPUS:85036546359

VL - 107

SP - 249

EP - 264

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 2

ER -