Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Rangarajan, E.S.; Ruane, K.M.; Proteau, A.; Schrag, J.D.; Valladares, R.; Gonzalez, C.F.; Gilbert, M.; Yakunin, A.F.; Cygler, M.
    Structural and enzymatic characterization of NanS (YjhS), a 9-O-acetyl N-acetylneuraminic acid esterase from Escherichia coli O157:H7 (2011), Protein Sci., 20, 1208-1219.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.53 purified wild-type apo-NanS and SeMet-labeled NanS, mixing of 0.001 ml of protein in the final buffer with 0.001 ml of reservoir solution containing 0.2 M NaCl, 0.1 M Bis-Tris pH 5.5, 30% w/v PEG 3350, in micro batch experiments under oil, X-ray diffraction structure determination and analysis at 1.6-2.2 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.53 E26A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type NanS Escherichia coli
3.1.1.53 H301N site-directed mutagenesis, inactive mutant Escherichia coli
3.1.1.53 S19A site-directed mutagenesis, inactive mutant Escherichia coli
3.1.1.53 S300A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS Escherichia coli
3.1.1.53 T294A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS Escherichia coli
3.1.1.53 T294S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.53 N-acetyl-O-9-acetylneuraminate + H2O Escherichia coli contribution of Ser19 and His301 to catalysis, active site structure, overview N-acetylneuraminate + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.53 Escherichia coli
-
 gene nanS, part of the nanCMS operon
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.53 1.29
-
 substrate O-9-acetyl-GD3-S-phenyl, pH 7.2, 25°C Escherichia coli
3.1.1.53 2.31
-
 substrate N-acetyl-O-9-acetylneuraminate, pH 7.2, 25°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.53 4-nitrophenylacetate + H2O
-
 Escherichia coli 4-nitrophenol + acetate
-
 ?
3.1.1.53 additional information NanS is also active on phenylacetate, butylacetate, triacetin, and slightly on rosmarinic acid and propylacetate, substrate specificity, overview. NanS shows negligible aryl esterase activity with alpha-naphthyl acetate and alpha-naphthyl propionate as substrates and no measurable lipolytic activity or thioesterase activity Escherichia coli ?
-
 ?
3.1.1.53 N-acetyl-O-9-acetylneuraminate + H2O best substrate Escherichia coli N-acetylneuraminate + acetate
-
 ?
3.1.1.53 N-acetyl-O-9-acetylneuraminate + H2O contribution of Ser19 and His301 to catalysis, active site structure, overview Escherichia coli N-acetylneuraminate + acetate
-
 ?
3.1.1.53 O-9-acetyl-GD3-S-phenyl + H2O i.e. 9-O-acetyl-NeuAcalpha-2,8-NeuAcalpha-2,3-Galbeta-1,4-Glcbeta-S-phenyl Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.53 monomer by gel filtration and dynamic light scattering, NanS adopts a SGNH hydrolase fold. The monomer has a central seven-stranded mixed beta-sheet with a strand order of beta5, beta2, beta6, beta1, beta9, beta10, beta11. Additionally, two beta-hairpins are present following strands beta2 and beta6. The N- and C-terminal alpha-helices, alpha1 and alpha7 respectively, are situated on the concave side of the beta-sheet while the remaining alpha-helices (alpha2, alpha4, and alpha6) are positioned on the convex side with alpha3 and alpha5 being one-turn 310-helices. Several extended loops are present on the concave side of the beta-sheet. One solvent exposed loop, Asn216-Thr218, located between alpha4 and beta6 is disordered in the structure Escherichia coli
3.1.1.53 More sequence motifs and two subfamilies of SGNH hydrolases, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.1.53 9-O-acetyl N-acetylneuraminic acid esterase
-
 Escherichia coli
3.1.1.53 More NanS belongs to the SGNH superfamily of hydrolases Escherichia coli
3.1.1.53 NANS
-
 Escherichia coli
3.1.1.53 YjhS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.53 25
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.53 7.2
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
3.1.1.53 evolution 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. Sequence motifs and two subfamilies of SGNH hydrolases, overview Escherichia coli
3.1.1.53 additional information the NanS catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad Escherichia coli