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• W2056404927 endingPage "606" @default.
• W2056404927 startingPage "593" @default.
• W2056404927 abstract "Esterases and deacetylases active on carbohydrate ligands have been classified into 14 families based upon amino acid sequence similarities. Enzymes from carbohydrate esterase family seven (CE-7) are unusual in that they display activity towards both acetylated xylooligosaccharides and the antibiotic, cephalosporin C. The 1.9A structure of the multifunctional CE-7 esterase (hereinafter CAH) from Bacillus subtilis 168 reveals a classical alpha/beta hydrolase fold encased within a 32 hexamer. This is the first example of a hexameric alpha/beta hydrolase and is further evidence of the versatility of this particular fold, which is used in a wide variety of biological contexts. A narrow entrance tunnel leads to the centre of the molecule, where the six active-centre catalytic triads point towards the tunnel interior and thus are sequestered away from cytoplasmic contents. By analogy to self-compartmentalising proteases, the tunnel entrance may function to hinder access of large substrates to the poly-specific active centre. This would explain the observation that the enzyme is active on a variety of small, acetylated molecules. The structure of an active site mutant in complex with the reaction product, acetate, reveals details of the putative oxyanion binding site, and suggests that substrates bind predominantly through non-specific contacts with protein hydrophobic residues. Protein residues involved in catalysis are tethered by interactions with protein excursions from the canonical alpha/beta hydrolase fold. These excursions also mediate quaternary structure maintenance, so it would appear that catalytic competence is only achieved on protein multimerisation. We suggest that the acetyl xylan esterase (EC 3.1.1.72) and cephalosporin C deacetylase (EC 3.1.1.41) enzymes of the CE-7 family represent a single class of proteins with a multifunctional deacetylase activity against a range of small substrates." @default.
• W2056404927 created "2016-06-24" @default.
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• W2056404927 date "2003-07-01" @default.
• W2056404927 modified "2023-09-23" @default.
• W2056404927 title "Multifunctional Xylooligosaccharide/Cephalosporin C Deacetylase Revealed by the Hexameric Structure of the Bacillus subtilis Enzyme at 1.9Å Resolution" @default.
• W2056404927 cites W1004997917 @default.
• W2056404927 cites W1539796472 @default.
• W2056404927 cites W1546206690 @default.
• W2056404927 cites W1568211035 @default.
• W2056404927 cites W1570270309 @default.
• W2056404927 cites W1597832780 @default.
• W2056404927 cites W1669459870 @default.
• W2056404927 cites W1764151989 @default.
• W2056404927 cites W1830745998 @default.
• W2056404927 cites W1880132961 @default.
• W2056404927 cites W1959789663 @default.
• W2056404927 cites W1975460230 @default.
• W2056404927 cites W1975993749 @default.
• W2056404927 cites W1977832025 @default.
• W2056404927 cites W1985374711 @default.
• W2056404927 cites W1987202977 @default.
• W2056404927 cites W1987435352 @default.
• W2056404927 cites W1989089713 @default.
• W2056404927 cites W1995278899 @default.
• W2056404927 cites W1996471792 @default.
• W2056404927 cites W1996607909 @default.
• W2056404927 cites W2000029034 @default.
• W2056404927 cites W2000511735 @default.
• W2056404927 cites W2001641653 @default.
• W2056404927 cites W2004370807 @default.
• W2056404927 cites W2009674285 @default.
• W2056404927 cites W2013181909 @default.
• W2056404927 cites W2013900027 @default.
• W2056404927 cites W2014694459 @default.
• W2056404927 cites W2018175631 @default.
• W2056404927 cites W2018964006 @default.
• W2056404927 cites W2028231353 @default.
• W2056404927 cites W2033784547 @default.
• W2056404927 cites W2036371153 @default.
• W2056404927 cites W2036414218 @default.
• W2056404927 cites W2038840577 @default.
• W2056404927 cites W2039585314 @default.
• W2056404927 cites W2042471904 @default.
• W2056404927 cites W2043121500 @default.
• W2056404927 cites W2047930189 @default.
• W2056404927 cites W2053363400 @default.
• W2056404927 cites W2058075084 @default.
• W2056404927 cites W2063142947 @default.
• W2056404927 cites W2063916577 @default.
• W2056404927 cites W2067698303 @default.
• W2056404927 cites W2078248419 @default.
• W2056404927 cites W2080476827 @default.
• W2056404927 cites W2084131741 @default.
• W2056404927 cites W2084575458 @default.
• W2056404927 cites W2085322299 @default.
• W2056404927 cites W2089292410 @default.
• W2056404927 cites W2092295455 @default.
• W2056404927 cites W2095303752 @default.
• W2056404927 cites W2097493124 @default.
• W2056404927 cites W2100312564 @default.
• W2056404927 cites W2102645001 @default.
• W2056404927 cites W2106297159 @default.
• W2056404927 cites W2108050742 @default.
• W2056404927 cites W2114618967 @default.
• W2056404927 cites W2117985613 @default.
• W2056404927 cites W2127708008 @default.
• W2056404927 cites W2128516811 @default.
• W2056404927 cites W2128649005 @default.
• W2056404927 cites W2145571109 @default.
• W2056404927 cites W2155157445 @default.
• W2056404927 cites W2164320858 @default.
• W2056404927 cites W2414307244 @default.
• W2056404927 cites W94004571 @default.
• W2056404927 doi "https://doi.org/10.1016/s0022-2836(03)00632-6" @default.
• W2056404927 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12842474" @default.
• W2056404927 hasPublicationYear "2003" @default.
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