1998
DOI: 10.1104/pp.117.1.153
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Rhamnogalacturonan α-d-Galactopyranosyluronohydrolase1

Abstract: A new enzyme, rhamnogalacturonan (RG) ␣-D-galactopyranosyluronohydrolase (RG-galacturonohydrolase), able to release a galacturonic acid residue from the nonreducing end of RG chains but not from homogalacturonan, was purified from an Aspergillus aculeatus enzyme preparation. RG-galacturonohydrolase acted with inversion of anomeric configuration, initially releasing ␤-Dgalactopyranosyluronic acid. The enzyme cleaved smaller RG substrates with the highest catalytic efficiency. A Michaelis constant of 85 M and a … Show more

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Cited by 58 publications
(19 citation statements)
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“…Rhamnogalacturonan galacturono hydrolase is able to release a GalA moiety connected to a rhamnose residue from the non-reducing side of RGI chains but is unable to liberate GalA from HG [82]. Similar to RGRH no sequence information for RGGH is available.…”
Section: Rhamnogalacturonan Galacturono Hydrolase (Rggh)mentioning
confidence: 99%
“…Rhamnogalacturonan galacturono hydrolase is able to release a GalA moiety connected to a rhamnose residue from the non-reducing side of RGI chains but is unable to liberate GalA from HG [82]. Similar to RGRH no sequence information for RGGH is available.…”
Section: Rhamnogalacturonan Galacturono Hydrolase (Rggh)mentioning
confidence: 99%
“…Breakdown of rhamnogalacturonan is mainly mediated by two rhamnogalacturonan-degrading enzymes, rhamnogalacturonan hydrolase (RGaseA) and rhamnogalacturonan lyase (RGaseB). The rhamnogalacturonandegrading system of Aspergillus aculeatus has been well characterized, and three-dimensional structures of RGaseA and RGaseB have been elucidated, contributing toward the understanding of their structure-function relationship (Kofod et al, 1994, Mutter et al, 1994, Mutter et al, 1996a, Mutter et al, 1996b, Mutter et al, 1998, McDonough et al, 2004, Jensen et al, 2010. Furthermore, the usefulness of these enzymes in the processing of food has been confirmed.…”
mentioning
confidence: 91%
“…The family 4 polysaccharide lyase, rhamnogalacturonan lyase (RG-lyase), which cleaves the a-1,4 backbone of RG-I through a b-elimination mechanism, has also been isolated from A. aculeatus (EC 4.2.2., SwissProt Q00019) [10][11][12]. Both RG-lyase and RG-hydrolase display an increase in catalytic efficiency towards deacetylated RG-I, thus these enzymes work synergistically with RGAE to degrade RG-I [13].…”
Section: Introductionmentioning
confidence: 99%
“…Cleavage via b-elimination introduces a double bond in the fourth residue, GalUA [14]. Removal of the branching galactan side chains FEBS Letters 565 (2004) attached to Rha decreases the enzymes catalytic efficiency, whereas removal of the branching arabinan side chains results in an increase in enzymatic efficiency [11]. Out of the 14 current polysaccharide lyase families, structures are known for families 1, 3, 5, 6, 7, 8, 9, and 10 [6].…”
Section: Introductionmentioning
confidence: 99%