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PMID: 9048892 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Biochimica et biophysica acta ·Vol. 1337 ·No. 2 ·1997-02-08 ·Pages 161-5

Flint HJ, Whitehead TR, Martin JC, Gasparic A

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Binding Sites DNA, Bacterial/genetics Genes, Bacterial Molecular Sequence Data Molecular Structure Prevotella/enzymology,genetics Rumen/microbiology Xylan Endo-1,3-beta-Xylosidase Xylosidases/chemistry,genetics
Chemicals
DNA, Bacterial Xylosidases Xylan Endo-1,3-beta-Xylosidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Flint H J
Rowett Research Institute, Bucksburn, Aberdeen, UK. [email protected]
Whitehead T R
Martin J C
Gasparic A
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1997-02-08
Pages
161-5
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Databases
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