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evolution
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
evolution
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
evolution
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
evolution
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
evolution
the enzyme belongs to the the PL-17 family
evolution
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the enzyme belongs to the to the polysaccharide lyase-7 family
evolution
the enzyme contains the conserved amino acid sequences RTELREM, QIH, and YFKAGVYNQ of the polysaccharide lyase family 7
evolution
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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
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evolution
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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
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evolution
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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
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evolution
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the enzyme belongs to the the PL-17 family
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physiological function
knockout mutant shows growth rates similar to wild-type in MB medium, but grows very slowly in the ASW liquid medium supplemented with 0.3% alginate
physiological 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
physiological function
Bacillus sp. TAG8 is able to utilize alginate as a sole carbon source
physiological function
deletion of the noncatalytic region of Aly1 causes weak changes of biochemical characteristics but increases the degradation proportions of small size-defined saturated M-enriched oligosaccharide substrates and unsaturated tetrasaccharide fractions without any size changes of degradable oligosaccharides
physiological function
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knockout mutant shows growth rates similar to wild-type in MB medium, but grows very slowly in the ASW liquid medium supplemented with 0.3% alginate
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additional information
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
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secondary structure comparison of AlyA5 and AlyA1PL7
additional information
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secondary structure comparison of AlyA5 and AlyA1PL7
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