S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE FROM XENOPUS-LAEVIS - IDENTIFICATION, DEVELOPMENTAL EXPRESSION AND EVOLUTION

Citation
Lt. Seery et al., S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE FROM XENOPUS-LAEVIS - IDENTIFICATION, DEVELOPMENTAL EXPRESSION AND EVOLUTION, Biochemical and biophysical research communications, 205(3), 1994, pp. 1539-1546
Citations number
29
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
205
Issue
3
Year of publication
1994
Pages
1539 - 1546
Database
ISI
SICI code
0006-291X(1994)205:3<1539:SHFX-I>2.0.ZU;2-B
Abstract
S-Adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) is an important enzym e in the trans-sulphuration pathway, mediating the conversion of S-ade nosyl-L-homocysteine to adenosine and L-homocysteine. We have identifi ed a cDNA clone from Xenopus laevis, encoding a protein of 433 aa, whi ch is highly conserved with S-Adenosyl-L-homocysteine hydrolases (Adoh cyases) from other species. Expression of Adohcyase mRNA in X.laevis t adpoles is detectable from developmental Stage 27 onwards. Phylogeneti c analysis of available Adohcyase sequences indicates that species clu ster essentially as predicted from morphological data. Furthermore, we estimate that S-adenosyl-L-homocysteine hydrolase is evolving very sl owly, almost 10 times slower than the average rate. (C) 1994 Academic Press, Inc.