In order to make further progress in elucidating the mechanism of
NOS catalysis it will be essential to throw light on the
interaction between the enzyme and its substrate. An understanding
of the catalytic site will also assist the development of
therapeutically important NOS inhibitors. In particular. it will be
useful to uncover any differences that exist between the substrate
binding sites of the three NOS isozymes which might be exploited
for the development of isoform selective NOS inhibitors. A
comparison of NOS to other Arg-binding proteins has shown no
significant sequence homology (159). Moreover, the lack of a 3D
structure and absence of significant sequence homology between the
NOS oxygenase domain and known cytochromes P450 has made it
difficult to identify residues and construct a model of the distal
heme pocket responsible for substrate binding. However, a number of
groups are currently working towards crystallisation of the
separate NOS reductase and oxygenase domains of the three isoforms
for X-ray diffraction studies; the first X-ray structure is likely
to be forthcoming within a matter of months. * The results of these
studies are expected to resolve many of the uncertainties
surrounding the structure of the NOS catalytic site. Preliminary
X-ray diffraction analysis of CPR from rat liver has already been
reported by MASTERS et al. (524) and the future emergence of a
detailed structure for this protein should throw light on the
structure and function of the NOS reductase domain.
General
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