Any feedback?
Literature summary for 3.1.1.53 extracted from
- 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.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| E26A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type NanS | Escherichia coli |
| H301N | site-directed mutagenesis, inactive mutant | Escherichia coli |
| S19A | site-directed mutagenesis, inactive mutant | Escherichia coli |
| S300A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS | Escherichia coli |
| T294A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS | Escherichia coli |
| T294S | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acetyl-O-9-acetylneuraminate + H2O | Escherichia coli | contribution of Ser19 and His301 to catalysis, active site structure, overview | N-acetylneuraminate + acetate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
gene nanS, part of the nanCMS operon | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.29 | - |
substrate O-9-acetyl-GD3-S-phenyl, pH 7.2, 25°C | Escherichia coli |
| 2.31 | - |
substrate N-acetyl-O-9-acetylneuraminate, pH 7.2, 25°C | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenylacetate + H2O | - |
Escherichia coli | 4-nitrophenol + acetate | - |
? | |
| 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 | ? | - |
? | |
| N-acetyl-O-9-acetylneuraminate + H2O | best substrate | Escherichia coli | N-acetylneuraminate + acetate | - |
? | |
| N-acetyl-O-9-acetylneuraminate + H2O | contribution of Ser19 and His301 to catalysis, active site structure, overview | Escherichia coli | N-acetylneuraminate + acetate | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
| More | sequence motifs and two subfamilies of SGNH hydrolases, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 9-O-acetyl N-acetylneuraminic acid esterase | - |
Escherichia coli |
| More | NanS belongs to the SGNH superfamily of hydrolases | Escherichia coli |
| NANS | - |
Escherichia coli |
| YjhS | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| additional information | the NanS catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
