Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

4.2.2.23: rhamnogalacturonan endolyase

This is an abbreviated version!
For detailed information about rhamnogalacturonan endolyase, go to the full flat file.

Word Map on EC 4.2.2.23

Reaction

Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. =

Synonyms

101259106, alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase, RG lyase, RG-lyase, RGase B, Rgl11A, Rgl11Y, RGL4, Rgl4A, RglA, RglF, rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase, rhamnogalacturonan lyase A, rhamnogalacturonase B, RhiE, Solyc11g011300, YesW

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.23 rhamnogalacturonan endolyase

Cloned

Cloned on EC 4.2.2.23 - rhamnogalacturonan endolyase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus oryzae
expression in Escherichia coli
expression in Escherichia coli and Bacillus subtilis strain natto
expression in Escherichia coli. Expression of the three modules of the Pseudomonas protein in Escherichia coli shows that its C-terminal module is a functional cellulose-binding domain, and the N-terminal module consists of a catalytic domain that hydrolyzes rhamnogalacturonan-containing substrates