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Literature summary for 3.5.1.42 extracted from
- Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases (2014), FEBS Lett., 588, 1016-1023.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene pncC, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E28A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Escherichia coli |
| K61Q | site-directed mutagenesis, inactive mutant | Escherichia coli |
| R142A | site-directed mutagenesis, inactive mutant | Escherichia coli |
| S103A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Escherichia coli |
| S29A | site-directed mutagenesis, inactive mutant | Escherichia coli |
| T31A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Escherichia coli |
| Y56A | site-directed mutagenesis, inactive mutant | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition by PMSF and desthiobiotin-fluorophosphonate | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Escherichia coli | |
| 0.007 | - |
beta-nicotinamide D-ribonucleotide | recombinant wild-type enzyme, pH 7.5, 37°C | Escherichia coli |  |
| 0.012 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant S103A, pH 7.5, 37°C | Escherichia coli | |
| 0.027 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant T31A, pH 7.5, 37°C | Escherichia coli | |
| 0.272 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant E28A, pH 7.5, 37°C | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-nicotinamide D-ribonucleotide + H2O | Escherichia coli | - |
beta-nicotinate D-ribonucleotide + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
gene pncC | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nicke affinity chromatography | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate D-ribonucleotide + NH3 | proposed mechanism of nicotinamide D-ribonucleotide deamidation by the enzyme via three reaction intermediates, which is a Ser/Lys hydrolase employing a Ser/Lys catalytic dyad, active site structure, overview | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-nicotinamide D-ribonucleotide + H2O | - |
Escherichia coli | beta-nicotinate D-ribonucleotide + NH3 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme structure comparisons | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NMN deamidase | - |
Escherichia coli |
| PncC | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
purified proteins, wild-type enzyme loses 40% activity after 20 min, 60% after 40 min, and 80% after 60 min, the mutant E28A lose s 50%, 80% and over 90% activity after 30, 40 qnd 60 min, the mutant T31A is inactivated within 20 min | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.1 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant S103A, pH 7.5, 37°C | Escherichia coli | |
| 3.2 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant T31A, pH 7.5, 37°C | Escherichia coli | |
| 3.9 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant E28A, pH 7.5, 37°C | Escherichia coli | |
| 4.1 | - |
beta-nicotinamide D-ribonucleotide | recombinant wild-type enzyme, pH 7.5, 37°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the PncC superfamily, active site configuration, structure comparisons, overview | Escherichia coli |
| additional information | enzyme surface charge analysis and substrate docking performed on the enzyme structure from Agrobacterium tumefaciens, PDB code 2A9S, overview | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 10 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant E28A, pH 7.5, 37°C | Escherichia coli | |
| 90 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant S103A, pH 7.5, 37°C | Escherichia coli | |
| 120 | - |
beta-nicotinamide D-ribonucleotide | recombinant mutant T31A, pH 7.5, 37°C | Escherichia coli | |
| 590 | - |
beta-nicotinamide D-ribonucleotide | recombinant wild-type enzyme, pH 7.5, 37°C | Escherichia coli | |
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