Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex

Satoshi Kaneko, Hitomi Ichinose, Zui Fujimoto, Atsushi Kuno, Kei Yura, Mitiko Go, Hiroshi Mizuno, Isao Kusakabe, Hideyuki Kobayashi

研究成果: Article

17 引用 (Scopus)

抄録

The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CgXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.

元の言語English
ページ(範囲)26619-26626
ページ数8
ジャーナルJournal of Biological Chemistry
279
発行部数25
DOI
出版物ステータスPublished - 2004 6 18
外部発表Yes

Fingerprint

Cellulomonas
Glycoside Hydrolases
Streptomyces
Substrates
Catalytic Domain
Enzymes
Topology
Biochemistry
Xylose
Hydrolysis
Genes
Crystal structure
Inspection
Amino Acids

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex. / Kaneko, Satoshi; Ichinose, Hitomi; Fujimoto, Zui; Kuno, Atsushi; Yura, Kei; Go, Mitiko; Mizuno, Hiroshi; Kusakabe, Isao; Kobayashi, Hideyuki.

:: Journal of Biological Chemistry, 巻 279, 番号 25, 18.06.2004, p. 26619-26626.

研究成果: Article

Kaneko, S, Ichinose, H, Fujimoto, Z, Kuno, A, Yura, K, Go, M, Mizuno, H, Kusakabe, I & Kobayashi, H 2004, 'Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex', Journal of Biological Chemistry, 巻. 279, 番号 25, pp. 26619-26626. https://doi.org/10.1074/jbc.M308899200
Kaneko, Satoshi ; Ichinose, Hitomi ; Fujimoto, Zui ; Kuno, Atsushi ; Yura, Kei ; Go, Mitiko ; Mizuno, Hiroshi ; Kusakabe, Isao ; Kobayashi, Hideyuki. / Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex. :: Journal of Biological Chemistry. 2004 ; 巻 279, 番号 25. pp. 26619-26626.
@article{00f4c3e9277247dd9a707e4061238acd,
title = "Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex",
abstract = "The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CgXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.",
author = "Satoshi Kaneko and Hitomi Ichinose and Zui Fujimoto and Atsushi Kuno and Kei Yura and Mitiko Go and Hiroshi Mizuno and Isao Kusakabe and Hideyuki Kobayashi",
year = "2004",
month = "6",
day = "18",
doi = "10.1074/jbc.M308899200",
language = "English",
volume = "279",
pages = "26619--26626",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "25",

}

TY - JOUR

T1 - Structure and function of a family 10 β-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi cex

AU - Kaneko, Satoshi

AU - Ichinose, Hitomi

AU - Fujimoto, Zui

AU - Kuno, Atsushi

AU - Yura, Kei

AU - Go, Mitiko

AU - Mizuno, Hiroshi

AU - Kusakabe, Isao

AU - Kobayashi, Hideyuki

PY - 2004/6/18

Y1 - 2004/6/18

N2 - The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CgXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.

AB - The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CgXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.

UR - http://www.scopus.com/inward/record.url?scp=2942754001&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2942754001&partnerID=8YFLogxK

U2 - 10.1074/jbc.M308899200

DO - 10.1074/jbc.M308899200

M3 - Article

C2 - 15078885

AN - SCOPUS:2942754001

VL - 279

SP - 26619

EP - 26626

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 25

ER -