The gene encoding
S-a
denosylhomocysteine hydrolase activity (SAHase: EC 3.3.1.1)
from
Corynebacterium efficiens (YS-314) was cloned and expressed as a
fusion protein in
Escherichiacoli Rosetta (DE3). The analyzed nucleoti
de sequence o
f the cloned gene proved to be i
denticalto those reported on the NCBI database. The recombinant enzyme is a tetramer, showing amolecular weight o
f approximately 210 kDa, as estimated by gel
filtration. The
KM values o
fthe enzyme
for
S-a
denosylhomocysteine (SAH), a
denosine (Ado), and homocysteine (Hcy), were
determined to be 1.4, 10, and 45
![](/images/entities/mgr.gi<font color=)
f">M. The overexpression o
f the recombinant enzyme produceda high level o
f protein (>40 mg o
f protein per gram o
f wet cells) and revealed certainthermostability when characterized at temperatures above 40
![](/images/entities/<font color=)
deg.gi
f">C. It also showed a high capacity
for the synthesis o
f SAH, thermal stability, and high kinetic similarity to human SAHase,indicating a high biotechnological and pharmacological potential.