Sequence determination and analysis of S-adenosyl-L-homocysteine hydrolase from yellow lupine (Lupinus luteus).

K Brzeziński; R Janowski; J Podkowiński; M Jaskólski

doi:10.18388/abp.2001_3931

Sequence determination and analysis of S-adenosyl-L-homocysteine hydrolase from yellow lupine (Lupinus luteus).

K Brzeziński Department of Crystallography, Faculty of Chemistry, Adam Mickiewicz University, Poznań, Poland.;
R Janowski
J Podkowiński
M Jaskólski

DOI: https://doi.org/10.18388/abp.2001_3931

Abstract

The coding sequences of two S-adenosyl-L-homocysteine hydrolases (SAHases) were identified in yellow lupine by screenig of a cDNA library. One of them, corresponding to the complete protein, was sequenced and compared with 52 other SAHase sequences. Phylogenetic analysis of these proteins identified three groups of the enzymes. Group A comprises only bacterial sequences. Group B is subdivided into two subgroups, one of which (B1) is formed by animal sequences. Subgroup B2 consist of two distinct clusters, B2a and B2b. Cluster B2b comprises all known plant sequences, including the yellow lupine enzyme, which are distinguished by a 50-residue insert. Group C is heterogeneous and contains SAHases from Archaea as well as a new class of animal enzymes, distinctly different from those in group B1.

Published

2001-06-30

Issue

Vol. 48 No. 2 (2001)

Section

Articles

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