To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
The following phosphorylases belongs to the same family:
Purine nucleoside phosphorylase (EC 22.214.171.124) (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 126.96.36.199) (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.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.