FEBS Letters
Volume 581, Issue 7 , Pages 1261-1268, 3 April 2007

A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31

Edited by Hans Eklund

  • Štefan Janeček

      Affiliations

    • Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21, SK-84551 Bratislava, Slovakia
    • Corresponding Author InformationCorresponding author. Fax: +421 2 5930 7416.
  • ,
  • Birte Svensson

      Affiliations

    • Enzyme and Protein Chemistry, BioCentrum-DTU, Technical University of Denmark, Søltofts Plads, DK-2800 Kgs. Lyngby, Denmark
  • ,
  • E. Ann MacGregor

      Affiliations

    • 2 Nicklaus Green, Livingston, EH54 8RX, West Lothian, UK

Received 11 December 2006; received in revised form 2 February 2007; accepted 19 February 2007. published online 01 March 2007.

Abstract 

Although both the α-amylase super-family, i.e. the glycoside hydrolase (GH) clan GH-H (the GH families 13, 70 and 77), and family GH31 share some characteristics, their different catalytic machinery prevents classification of GH31 in clan GH-H. A significant but remote evolutionary relatedness is, however, proposed for clan GH-H with GH31. A sequence alignment, based on the idea that residues equivalent in the primordial catalytic GH-H/GH31 (β/α)8-barrel may not be found in the present-day GH-H and GH31 structures at strictly equivalent positions, shows remote sequence homologies covering β3, β4, β7 and β8 of the GH-H and GH31 (β/α)8-barrels. Structure comparison of GH13 α-amylase and GH31 α-xylosidase guided alignment of GH-H and GH31 members for construction of evolutionary trees. The closest sequence relationship displayed by GH31 is to GH77 of clan GH-H.

Abbreviations: GH, glycoside hydrolase, TIM, triose phosphate isomerase

Keywords: α-Amylase, α-Xylosidase, Glycoside hydrolase family 13, Glycoside hydrolase family 31, Structural alignment, Remote homology, Evolutionary tree

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(07)00202-5

doi:10.1016/j.febslet.2007.02.036

FEBS Letters
Volume 581, Issue 7 , Pages 1261-1268, 3 April 2007