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
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.