1998
DOI: 10.1016/s0008-6215(98)00188-8
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Mode of action of RG-hydrolase and RG-lyase toward rhamnogalacturonan oligomers. Characterization of degradation products using RG-rhamnohydrolase and RG-galacturonohydrolase1Financed by Novo Nordisk A/S, Bagsvaerd, Denmark.1

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Cited by 64 publications
(35 citation statements)
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“…By analogy, Rha 1501 bound in the active site of SaRha78A appears to be migrating between the transition state and product conformations adopted during the reaction trajectory. Thus, it would appear that a boat 2,5 B is the conformation adopted by the transition state of glycans hydrolyzed by GH78 rhamnosidases. It is interesting to note that although Cui et al (7) were unable to model an L-rhamnose in its relaxed confirmation into the active site electron density, the authors suggested that this may be because the bound sugar adopted a distorted conformation, as observed here.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…By analogy, Rha 1501 bound in the active site of SaRha78A appears to be migrating between the transition state and product conformations adopted during the reaction trajectory. Thus, it would appear that a boat 2,5 B is the conformation adopted by the transition state of glycans hydrolyzed by GH78 rhamnosidases. It is interesting to note that although Cui et al (7) were unable to model an L-rhamnose in its relaxed confirmation into the active site electron density, the authors suggested that this may be because the bound sugar adopted a distorted conformation, as observed here.…”
Section: Discussionmentioning
confidence: 99%
“…L-Rhamnose is widely distributed in plants and bacteria as a component of polysaccharides, such as rhamnogalacturonan and arabinogalactan-protein (1,2), whereas the sugar is also found in some glycol conjugates such as naringin and rutin (3,4). Naringin, a major flavonoid in grapefruit, contains ␣-1,2-linked L-rhamnose.…”
mentioning
confidence: 99%
“…To clarify the mode of action of YesW and YesX, the degradation profile of RG-I through the YesW or YesX reaction was analyzed by size-exclusion chromatography. Substrate RG chain suitable for this analysis was prepared from RG-I as described elsewhere (37). Briefly, 1 g of de-esterified RG-I was hydrolyzed in 100 ml of 0.1 M HCl at 80°C for 72 h. The hydrolysate was neutralized with NaOH and centrifuged at 20,000 ϫ g for 10 min.…”
Section: Methodsmentioning
confidence: 99%
“…A large number of polygalacturonan-degrading enzymes (i.e., pectin lyase, pectate lyase, and polygalacturonase) have also been identified from many fungi and bacteria, including B. subtilis (11,45). Reports on the microbial degradation system for the RG region in pectin have been limited, however, except for A. aculeatus strain KSM 510 (33)(34)(35)(36)(37), possibly due to the complex structure of the heteropolysaccharide, although a few RG lyases from fungi and bacteria have been identified (14,29,36,43). The analysis of RG degradation by B. subtilis is important for clarification of its saprophytic interaction with plants.…”
mentioning
confidence: 99%
“…RG galacturonohydrolase (EC 3.2.1.-) catalyzes hydrolytic cleavage of the rhamnogalacturonan chain at nonreducing end producing monogalacturonate [41]. It is classified into glycosyl-hydrolase family 28 [13].…”
Section: Rhamnogalcturonan Galacturonohydrolasesmentioning
confidence: 99%