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The following phosphorylases belongs to the same family:
Purine nucleoside phosphorylase (EC 188.8.131.52) (PNP) from mammals as well as
from some bacteria (gene deoD). This enzyme catalyzes the cleavage of
guanosine or inosine to respective bases and sugar-1-phosphate molecules
5'-methylthioadenosine phosphorylase (EC 184.108.40.206) (MTA phosphorylase) from
Xanthosine phosphorylase (EC 2.4.2.-) from Escherichia coli (gene xapA).
This enzyme can degrade all purine nucleosides except adenosine and
This family also includes the following uncharacterized proteins:
Yeast hypothetical protein YLR017w.
Fission yeast hypothetical protein SpAC16C9.02c.
Methanococcus jannaschii hypothetical protein MJ0060.
Rhodospirillum rubrum hypothetical protein in petC 3'region.
As a signature pattern, we selected a conserved region in the central part of
It should be noted that most bacterial PNP as well as archaebacterial
MTA phosphorylase belong to a different family of phosphorylases (see
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Ealick S.E., Rule S.A., Carter D.C., Greenhough T.J., Babu Y.S., Cook W.J., Habash J., Helliwell J.R., Stoeckler J.D., Parks R.E. Jr. Chen S.-F., Bugg C.E.
Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.
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