Structural and enzymatic characterization of NanS (YjhS), a 9-O-Acetyl N-acetylneuraminic acid esterase from Escherichia coli O157:H7

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DOIResolve DOI: http://doi.org/10.1002/pro.649
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TypeArticle
Journal titleProtein Science
Volume20
Issue7
Pages12081219; # of pages: 12
Subjectcarbohydrate esterase; crystal structure; SGNH hydrolase; sialic acid; substrate profile
AbstractThere is a high prevalence of sialic acid in a number of different organisms, resulting in there being a myriad of different enzymes that can exploit it as a fermentable carbon source. One such enzyme is NanS, a carbohydrate esterase that we show here deacetylates the 9 position of 9-O-sialic acid so that it can be readily transported into the cell for catabolism. Through structural studies, we show that NanS adopts a SGNH hydrolase fold. Although the backbone of the structure is similar to previously characterized family members, sequence comparisons indicate that this family can be further subdivided into two subfamilies with somewhat different fingerprints. NanS is the founding member of group II. Its catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad. The contribution of Ser19 and His301 to catalysis was confirmed by mutagenesis. In addition to structural characterization, we have mapped the specificity of NanS using a battery of substrates.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Biotechnology Research Institute; NRC Institute for Biological Sciences
Peer reviewedYes
NRC number53145
NPARC number18178002
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Record identifier66139cbd-80de-4152-a7db-7fe401957310
Record created2011-07-28
Record modified2017-03-23
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