Catalytic metal coordination in CSAS enzymes



 Deference in Motif V suggests that insect CSASs coordinate metal cofactors differently from counterparts in vertebrates and bacteria.
The first aspartic acid of
the DID triad (*)
is required for coordinating
a catalytic metal cofactor
in the active site of
bacterial and vertebrate
CSAS enzymes. Site-directed
mutagenesis suggests that
the third D of the EID triad
is essential for metal
coordination in insect CSAS
(Mertsalov et al. 2016).

<--- back to previous page