Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
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
Pectinesterase (EC 184.108.40.206) (pectin methylesterase) catalyzes the hydrolysis
of pectin into pectate and methanol. In plants, it plays an important role in
cell wall metabolism during fruit ripening, cell wall extension and during
pollen germination. In plant bacterial pathogens such as Erwinia carotovora
and in fungal pathogens such as Aspergillus niger, pectinesterase is involved
in maceration and soft-rotting of plant tissue.
Prokaryotic and eukaryotic pectinesterases share a few regions of sequence
similarity [1,2,3]. We selected two of these regions as signature patterns.
The first is based on a region in the N-terminal section of these enzymes; it
contains a conserved tyrosine which may play a role in the catalytic mechanism
. The second pattern corresponds to the conserved sequence around an active
site aspartate , an octapeptide located in the central part of these
June 2002 / Text revised.
PROSITE methods (with tools and information) covered by this documentation:
Ray J., Knapp J., Grierson D., Bird C., Schuch W.
Identification and sequence determination of a cDNA clone for tomato pectin esterase.
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.