The gene enco
ding
S-a
denosylhomocysteine hy
drolase activity (SAHase: EC 3.3.1.1) from
Corynebacterium efficiens (YS-314) was clone
d an
d expresse
d as a fusion protein in
Escherichiacoli Rosetta (DE3). The analyze
d nucleoti
de sequence of the clone
d gene prove
d to be i
denticalto those reporte
d on the NCBI
database. The recombinant enzyme is a tetramer, showing amolecular weight of approximately 210 kDa, as estimate
d by gel filtration. The
KM values ofthe enzyme for
S-a
denosylhomocysteine (SAH), a
denosine (A
do), an
d homocysteine (Hcy), were
determine
d to be 1.4, 10, an
d 45
M. The overexpression of the recombinant enzyme pro
duce
da high level of protein (>40 mg of protein per gram of wet cells) an
d reveale
d certainthermostability when characterize
d at temperatures above 40
deg.gif">C. It also showe
d a high capacityfor the synthesis of SAH, thermal stability, an
d high kinetic similarity to human SAHase,in
dicating a high biotechnological an
d pharmacological potential.