Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain

Rodrigo Gutiérrez, Ella Cederlund, Lars Hjelmqvist, Alessandra Peirano, Francisco Herrera, Debashis Ghosh, William Duax, Hans Jörnvall, Jaime Eyzaguirre

Resultado de la investigación: Article

24 Citas (Scopus)

Resumen

Penicillium purpurogenum produces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2 gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei (67% residue identity) and putative active site residues are conserved, but the Penicillium enzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichoderma enzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichoderma esterase by gene fusion.

Idioma originalEnglish
Páginas (desde-hasta)35-38
Número de páginas4
PublicaciónFEBS Letters
Volumen423
N.º1
DOI
EstadoPublished - 13 feb 1998

Huella dactilar

acetylxylan esterase
Trichoderma
Penicillium
Esterases
Cellulose
Catalytic Domain
Genes
Gene Fusion
Enzymes
Protein Sorting Signals
Introns
Proteins
Fusion reactions
Complementary DNA
DNA

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Citar esto

Gutiérrez, Rodrigo ; Cederlund, Ella ; Hjelmqvist, Lars ; Peirano, Alessandra ; Herrera, Francisco ; Ghosh, Debashis ; Duax, William ; Jörnvall, Hans ; Eyzaguirre, Jaime. / Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain. En: FEBS Letters. 1998 ; Vol. 423, N.º 1. pp. 35-38.
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abstract = "Penicillium purpurogenum produces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2 gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei (67{\%} residue identity) and putative active site residues are conserved, but the Penicillium enzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichoderma enzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichoderma esterase by gene fusion.",
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Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain. / Gutiérrez, Rodrigo; Cederlund, Ella; Hjelmqvist, Lars; Peirano, Alessandra; Herrera, Francisco; Ghosh, Debashis; Duax, William; Jörnvall, Hans; Eyzaguirre, Jaime.

En: FEBS Letters, Vol. 423, N.º 1, 13.02.1998, p. 35-38.

Resultado de la investigación: Article

TY - JOUR

T1 - Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain

AU - Gutiérrez, Rodrigo

AU - Cederlund, Ella

AU - Hjelmqvist, Lars

AU - Peirano, Alessandra

AU - Herrera, Francisco

AU - Ghosh, Debashis

AU - Duax, William

AU - Jörnvall, Hans

AU - Eyzaguirre, Jaime

PY - 1998/2/13

Y1 - 1998/2/13

N2 - Penicillium purpurogenum produces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2 gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei (67% residue identity) and putative active site residues are conserved, but the Penicillium enzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichoderma enzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichoderma esterase by gene fusion.

AB - Penicillium purpurogenum produces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2 gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei (67% residue identity) and putative active site residues are conserved, but the Penicillium enzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichoderma enzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichoderma esterase by gene fusion.

KW - Acetyl xylan esterase

KW - Cellulose binding domain

KW - Gene fusion

KW - Penicillium purpurogenum

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