Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosacharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosacharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
responsible for an initial cleavage of the rhamnogalacturonan I region of plant cell wall pectin. Bacillus subtilis strain 168 secretes two rhamnogalacturonan lyases, YesW and YesX, extracellularly. YesW cleaves the glycoside bond of the rhamnogalacturonan chain endolytically, and the resultant oligosaccharides are subsequently converted to disaccharides, unsaturated galacturonyl rhamnose, through the exotype reaction of YesX
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-GalA bonds of rhamnogalacturonan I oligosacharides containing L-rhamnopyranose at the reducing end and 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
enzyme is an exo-type polysaccharide lyase that cleaves rhamnogalacturonan from the reducing end. The active site possesses an L-shaped cleft that can accommodate galactosyl side chains
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
the enzyme is part of the degradation system of rhamnogalacturonan type I. YesW catalyzes the initial cleavage of the rhamnogalacturonan I main chain, and the resultant oligosaccharides are converted to disaccharides through the extracellular exotype YesX reaction. The disaccharide is finally degraded into its constituent monosaccharides through the reaction of intracellular unsaturated galacturonyl hydrolases YesR and YteR
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
rhamnogalacturonan I from potatoes. YesX acts on the substrate exolytically and releases disaccharides as major product. The enzyme mainly acts on rhamnogalacturonan I backbone, slight activity on polygalacturonan
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
the enzyme is part of the degradation system of rhamnogalacturonan type I. YesW catalyzes the initial cleavage of the rhamnogalacturonan I main chain, and the resultant oligosaccharides are converted to disaccharides through the extracellular exotype YesX reaction. The disaccharide is finally degraded into its constituent monosaccharides through the reaction of intracellular unsaturated galacturonyl hydrolases YesR and YteR
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
rhamnogalacturonan I from potatoes. YesX acts on the substrate exolytically and releases disaccharides as major product. The enzyme mainly acts on rhamnogalacturonan I backbone, slight activity on polygalacturonan
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4,5-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
responsible for an initial cleavage of the rhamnogalacturonan I region of plant cell wall pectin. Bacillus subtilis strain 168 secretes two rhamnogalacturonan lyases, YesW and YesX, extracellularly. YesW cleaves the glycoside bond of the rhamnogalacturonan chain endolytically, and the resultant oligosaccharides are subsequently converted to disaccharides, unsaturated galacturonyl rhamnose, through the exotype reaction of YesX
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
the enzyme is part of the degradation system of rhamnogalacturonan type I. YesW catalyzes the initial cleavage of the rhamnogalacturonan I main chain, and the resultant oligosaccharides are converted to disaccharides through the extracellular exotype YesX reaction. The disaccharide is finally degraded into its constituent monosaccharides through the reaction of intracellular unsaturated galacturonyl hydrolases YesR and YteR
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end
the enzyme is part of the degradation system of rhamnogalacturonan type I. YesW catalyzes the initial cleavage of the rhamnogalacturonan I main chain, and the resultant oligosaccharides are converted to disaccharides through the extracellular exotype YesX reaction. The disaccharide is finally degraded into its constituent monosaccharides through the reaction of intracellular unsaturated galacturonyl hydrolases YesR and YteR
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, structure determined at 1.32 A and 1.65 resolution, respectively. YesX crystal belongs to space group P2(1)2(1)2(1) with unit cell parameters of a = 72.9 A, b = 88.1 A, and c = 99.3 A. One molecule is present in an asymmetric unit
in complex with substrates, to 2.85 A resolution. The substrate-binding site is in the clefts formed by domains II and III and not located near the subunit-interaction surface and the Ca2+-binding site
the mutant enzyme shows an endolytic reaction profile. Vmax/Km-value for the mutant enzyme is 275fold lower than the Vmax/KM-value for the wild-type enzyme