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Crystal structure of exo‐rhamnogalacturonan lyase from Penicillium chrysogenum Penicillium chrysogenum as a member of polysaccharide lyase family 26

机译:来自青霉植物植物植物中的Exo-rhamnogalactuRonan碱酶的晶体结构作为多糖裂解酶系列的成员26

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Exo‐rhamnogalacturonan lyase from Penicillium chrysogenum 31B (Pc RGLX ) was recently classified as a member of polysaccharide lyase ( PL ) family 26 along with hypothetical proteins derived from various organisms. In this study, we determined the crystal structure of Pc RGLX as the first structure of a member of this family. Based on the substrate‐binding orientation and substrate specificity, Pc RGLX is an exo‐type PL that cleaves rhamnogalacturonan from the reducing end. Analysis of Pc RGLX ‐complex structures with reaction products indicate that the active site possesses an L‐shaped cleft that can accommodate galactosyl side chains, suggesting side‐chain‐bypassing activity in Pc RGLX . Furthermore, we determined the residues critical for catalysis by analyzing the enzyme activities of inactive variants.
机译:从青霉钙瘤31b(pc rglx)的Exo-rhamnogalactulanan碱酶最近被分类为多糖裂解酶(Pl)家族26的成员以及来自各种生物的假设蛋白质。 在这项研究中,我们确定了PC RGLX的晶体结构作为本系成员的第一结构。 基于基质结合取向和底物特异性,PC RGLX是从还原末端切割鼠李杆菌属植物的外壳型PL。 用反应产物的PC rglx -complex结构的分析表明,活性位点具有L形裂缝,其可以容纳半乳糖基侧链,表明PC RGLX中的侧链旁路活性。 此外,我们通过分析惰性变体的酶活性来确定对催化的残留物至关重要。

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