Interrupted catalytic domain structures in xylanases from two distantly related strains of Prevotella ruminicola

H J Flint, T R Whitehead, J C Martin, A Gasparic

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Two xylanases from the rumen anaerobic bacterium Prevotella ruminicola were found to possess highly unusual structures in which family 10 catalytic domains are interrupted by unrelated sequences. XynC from P. ruminicola B(1)4 carries a 160 amino-acid insertion, while a P. ruminicola D31d xylanase carries an unrelated region of 280 amino acids, containing an imperfect 130 amino-acid duplication. Both regions of family 10 similarity were shown to be essential for activity of the D31d enzyme.

Original languageEnglish
Pages (from-to)161-165
Number of pages5
JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume1337
Issue number2
Publication statusPublished - 8 Feb 1997

Keywords

  • xylanase
  • rumen
  • domain structure
  • interrupting sequence
  • (P-ruminicola)
  • AMINO-ACID-SEQUENCE
  • BACTEROIDES-RUMINICOLA
  • PSEUDOMONAS-FLUORESCENS
  • CELLULOMONAS-FIMI
  • STREPTOMYCES-LIVIDANS
  • ENDOGLUCANASE GENE
  • CRYSTAL-STRUCTURE
  • ACTIVE-SITE
  • BACTERIA
  • FAMILIES

Cite this

Interrupted catalytic domain structures in xylanases from two distantly related strains of Prevotella ruminicola. / Flint, H J ; Whitehead, T R ; Martin, J C ; Gasparic, A .

In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1337, No. 2, 08.02.1997, p. 161-165.

Research output: Contribution to journalArticle

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AU - Gasparic, A

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