| Description | This entry describes purine nucleotide phosphorylases (PNPs). Some proteins in this entry have been shown to act on inosine and guanosine, though their physiological substrates and role in vivo are not known [ , ]. Closely related clades act on inosine and guanosine (PNPH, ), and xanthosine, inosine and guanosine (XAPA, ) neither of these will act on adenosine. A more distantly related clade (MTAP, ) acts on methylthioadenosine. The structure of the Cellulomonas enzyme ( ) has been determined [ ]. This enzyme is a homotrimer where the subunits appear to bind cooperatively and trimerisation occurs through both hydrogen bonding and hydrophobic interactions. The core of each subunit, like other trimeric PNPs, consists of a nine-stranded β sheet, though the surrounding helices are less well conserved. The postions and geometric arrangments of the three active sites of each trimer are also conserved with other trimeric PNPs. | Name | Putative purine nucleotide phosphorylase |
| Short Name | PUNP | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
