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Results 1 - 10 of 12 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution Alg2A belongs to the polysaccharide lyase family 7, but has a different endolytic reaction mode from other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A, overview 730135
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution AlyA1PL7 is an endolytic guluronate lyase and belongs to the PL7 family, subfamily 1, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism -, 730018
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism -, 730018
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview -, 730063
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution the enzyme belongs to the the PL-17 family -, 729056
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution the enzyme belongs to the to the polysaccharide lyase-7 family 729459
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11evolution the enzyme contains the conserved amino acid sequences RTELREM, QIH, and YFKAGVYNQ of the polysaccharide lyase family 7 730184
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11more secondary structure comparison of AlyA5 and AlyA1PL7 -, 730018
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11physiological function alginate lyase consists of three domains, i.e. a carbohydrate-binding domain, a family 32 CBM domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). The CBM32 domain does not contribute to enhancing AlyQ's activity under the assayed conditions but can bind to cleaved but not intact alginate. The CBM32 and catalytic domains do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1 749331
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.11physiological function Bacillus sp. TAG8 is able to utilize alginate as a sole carbon source 747995
Results 1 - 10 of 12 > >>