Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library

Ki Hyun Nam, Soo Jin Kim, Kwang Yeon Hwang

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes.

Original languageEnglish
Pages (from-to)183-186
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume383
Issue number2
DOIs
Publication statusPublished - 2009 May 29

Fingerprint

Metagenome
Crystal structure
Biomass
Enzymes
Multifunctional Enzymes
Carbon Cycle
Genetic engineering
Cellulases
Xylans
Degradation
Bioconversion
Proteins
Genetic Engineering
Glucans
Plant Cells
Hordeum
Cell Wall
Polysaccharides
Bacteria
Animals

Keywords

  • Bifunctional enzyme
  • CelM2
  • Glucanase
  • Glucanase-xylanase
  • Xylanase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library. / Nam, Ki Hyun; Kim, Soo Jin; Hwang, Kwang Yeon.

In: Biochemical and Biophysical Research Communications, Vol. 383, No. 2, 29.05.2009, p. 183-186.

Research output: Contribution to journalArticle

@article{888676661b424befaacafac22d971579,
title = "Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library",
abstract = "Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes.",
keywords = "Bifunctional enzyme, CelM2, Glucanase, Glucanase-xylanase, Xylanase",
author = "Nam, {Ki Hyun} and Kim, {Soo Jin} and Hwang, {Kwang Yeon}",
year = "2009",
month = "5",
day = "29",
doi = "10.1016/j.bbrc.2009.03.149",
language = "English",
volume = "383",
pages = "183--186",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "2",

}

TY - JOUR

T1 - Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library

AU - Nam, Ki Hyun

AU - Kim, Soo Jin

AU - Hwang, Kwang Yeon

PY - 2009/5/29

Y1 - 2009/5/29

N2 - Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes.

AB - Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes.

KW - Bifunctional enzyme

KW - CelM2

KW - Glucanase

KW - Glucanase-xylanase

KW - Xylanase

UR - http://www.scopus.com/inward/record.url?scp=65049087435&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=65049087435&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.03.149

DO - 10.1016/j.bbrc.2009.03.149

M3 - Article

C2 - 19345197

AN - SCOPUS:65049087435

VL - 383

SP - 183

EP - 186

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 2

ER -