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Figure 5.
FIGURE 5. Top, comparison of IIIb-A conformation as
observed in the crystals (phenylacetaldehyde derived carbon
atoms in cyan) with a more optimal configuration (IIIb-B) based
on the modeled intermediate IIIa (Fig. 1) during tryptamine
reduction (Ref. 8; phenylacetaldehyde-derived carbon atoms in
yellow). Putative hydrogen bonding interactions made between
IIIb-B conformation and active site residues are shown by dotted
lines. Key active site residues and TTQ cofactor are displayed
with green carbons. B, overlay of crystal structures of IIIb-A
(with green carbons) and Vc (with cyan carbons) for
phenylacetaldehyde and ammonia as substrates. The active site
water molecule situated close to C-6 and O-7 is shown as a red
sphere (labeled W-1[ox]and W-1[red], respectively).
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