- Encompasses the most recent advances within the box.
- New sequence editor, Daniel Purich, is a widely known biochemist and enzymologist.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology: And Related Areas of Molecular Biology, Volume 76
Pyogenes structure (water #179 in 1zfj) might actually be a cation, possibly NH4þ from crystallization buffer (19, 20). The apparently conserved role of a cation at site 1 may be stabilization of a particular loop 6 conformation related to hydride transfer, rather than direct participation in the reaction. The absence of a cation in the human complex with 6-Cl-IMP-modified enzyme may be due to reorientation of the loop, which would malform the cation binding site; however, the cofactor site is evidently preserved since the 6-Cl-IMP-inactivated enzyme binds the NAD analog SAD.
Coli enzyme has not been reported. The secondarystructure representation is taken from the S. pyogenes structure and appears to be representative of the other IMPDH. The residues that interact with IMP and NAD are marked with single asterisks and those that bind Kþ by exclamation points. The three residues initially found mutated in patient families with RP10 retinitis pigmentosa are designated with double asterisks. The active-site loop, flap, and subdomain are boxed. INOSINE 50 -MONOPHOSPHATE DEHYDROGENASE 13 Figure 6.
The recognition that IMPDH type 2 expression is enhanced in growing mammalian cells, such as tumor cells and proliferating lymphocytes, directed substantial attention to this enzyme as a target for inhibitory cancer chemotherapeutic and immunosuppressive agents (11). However, selective inhibition of IMPDH type 1 was recently shown to suffice for endothelial cell growth arrest resulting in inhibition of tumor angiogenesis (40). This observation contrasts with the predominant view that development of selective IMPDH type 2 inhibitors will improve their clinical utility.
Advances in Enzymology and Related Areas of Molecular Biology: And Related Areas of Molecular Biology, Volume 76