Crawl of outlinks from wikipedia.org started March, 2016. These files are currently not publicly accessible.
Properties of this collection.
It has been several years since the last time we did this.
For this collection, several things were done:
1. Turned off duplicate detection. This collection will be complete, as there is a
good chance we will share the data, and sharing data with pointers to random
other collections, is a complex problem.
2. For the first time, did all the different wikis. The original runs were just against the
enwiki. This one, the seed list was built from all 865 collections.
TIMESTAMPS
The Wayback Machine - https://web.archive.org/web/20160309023730/http://prosite.expasy.org/doc/PS00599
Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity,
these various enzymes can be grouped [1] into subfamilies. One of these,
called class-II, currently consists of the following enzymes:
Glycine C-acetyltransferase (EC 2.3.1.29), which catalyzes the addition of
acetyl-CoA to glycine to form 2-amino-3-oxobutanoate (gene kbl).
5-aminolevulinic acid synthase (EC 2.3.1.37) (delta-ALA synthase), which
catalyzes the first step in heme biosynthesis via the Shemin (or C4)
pathway, i.e. the addition of succinyl-CoA to glycine to form 5-
aminolevulinate.
8-amino-7-oxononanoate synthase (EC 2.3.1.47) (7-KAP synthase), a bacterial
enzyme (gene bioF) which catalyzes an intermediate step in the biosynthesis
of biotin: the addition of 6-carboxy-hexanoyl-CoA to alanine to form 8-
amino-7-oxononanoate.
Histidinol-phosphate aminotransferase (EC 2.6.1.9), which catalyzes the
eighth step in histidine biosynthetic pathway: the transfer of an amino
group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form
histidinol phosphate and 2-oxoglutarate.
Serine C-palmitoyltransferase (EC 2.3.1.50) from yeast (genes LCB1 and
LCB2), which catalyzes the condensation of palmitoyl-CoA and serine to form
3-ketosphinganine.
The sequence around the pyridoxal-phosphate attachment site of this class of
enzyme is sufficiently conserved to allow the creation of a specific pattern.
Last update:
December 2004 / Pattern and text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
Reference
1
Authors
Bairoch A.
Source
Unpublished observations (1991).
Copyright
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
Prosite License
or see: prosite_license.html.
