EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.7.1 | drug development | development of NMNATase inhibitors as potential therapeutics against tularemia | Francisella tularensis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.6.1.13 | expression of GST-tagged nezyme in Escherichia coli | Francisella tularensis |
3.6.1.13 | expression of the His-tagged enzyme in Escherichia coli strain Bl21 | Synechocystis sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.7.1 | the enzyme is complexed with the co-purified NAD and pyrophosphate in the NadM-domain active site, and with ADPR substrate in the Nudix-domain, X-ray diffraction structure determination and analysis at 2.6 A resolution | Synechocystis sp. |
2.7.7.1 | X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method, co-crystallization of ftNadM-Nudix complexed with the product AMP and Mn2+ ions in the Nudix active site | Francisella tularensis |
3.6.1.13 | purified recombinant enzyme in complex with the product AMP and Mn2+ ions in its Nudix active site, sitting drop vapor diffusion method, 20°C, 0.001 ml of 15 mg/ml protein solution is mixed with an equal volume of reservoir solution containing 0.1 M Tris, pH 7.5, 200 mM MgCl2, and 19% PEG 3350, with or without 30 mM AMP, equilibration against the reservoir, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method | Francisella tularensis |
3.6.1.13 | purified recombinant His-tagged enzyme in complex with co-purified NAD and diphosphate complexed in the NadM-domain active site, and with ADPR substrate complexed in the Nudix-domain, hanging drop vapor diffusion method, 0.0015 ml of 15 mg/ml protein solution is mixed with an equal volume of reservoir solution containing 100 mM Tris, pH 7.5, and 1.5 M Li2SO4, 20°C, 3 days to 2 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, selenomethionyl MAD phasing method | Synechocystis sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.1 | additional information | - |
additional information | steady state kinetics | Francisella tularensis | |
2.7.7.1 | additional information | - |
additional information | steady state kinetics | Synechocystis sp. | |
2.7.7.1 | 0.041 | - |
ADP-ribose | pH 8.2, 37°C | Francisella tularensis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.1 | Mg2+ | presence of a metal ion cluster in the active site of the enzyme's Nudix domain, structure analysis and determination of the metal ion positions | Francisella tularensis | |
2.7.7.1 | Mn2+ | presence of a metal ion cluster in the active site of the enzyme's Nudix domain, structure analysis and determination of the metal ion positions | Francisella tularensis | |
3.6.1.13 | Mg2+ | - |
Francisella tularensis | |
3.6.1.13 | Mg2+ | - |
Synechocystis sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.1 | ATP + NMN | Synechocystis sp. | the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways | diphosphate + NAD+ | - |
? | |
2.7.7.1 | ATP + NMN | Francisella tularensis | the enzyme likely plays a central role in the pathway of NAD de novo synthesis in Francisella tularensis | diphosphate + NAD+ | - |
? | |
3.6.1.13 | ADP-ribose + H2O | Francisella tularensis | - |
AMP + D-ribose 5-phosphate | - |
? | |
3.6.1.13 | ADP-ribose + H2O | Synechocystis sp. | - |
AMP + D-ribose 5-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.1 | Francisella tularensis | Q5NHR1 | - |
- |
2.7.7.1 | Synechocystis sp. | Q55928 | - |
- |
3.6.1.13 | Francisella tularensis | Q5NHR1 | - |
- |
3.6.1.13 | Synechocystis sp. | Q55928 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.6.1.13 | recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by TEV protease, and the detagged protein is further purified by anion exchange chromatography | Francisella tularensis |
3.6.1.13 | recombinant His-tagged enzyme from Escherichia coli strain Bl21 by nickel affinity and anion exchange chromatography, and gel filtration | Synechocystis sp. |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.7.7.1 | ATP + nicotinamide ribonucleotide = diphosphate + NAD+ | catalytic mechanism, overview | Francisella tularensis | |
2.7.7.1 | ATP + nicotinamide ribonucleotide = diphosphate + NAD+ | catalytic mechanism, overview | Synechocystis sp. | |
3.6.1.13 | ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate | substrate binding mode in the active site of the ADPRase domain and catalytic mechanism | Francisella tularensis | |
3.6.1.13 | ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate | substrate binding mode in the active site of the ADPRase domain and catalytic mechanism | Synechocystis sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.1 | ATP + NMN | the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways | Synechocystis sp. | diphosphate + NAD+ | - |
? | |
2.7.7.1 | ATP + NMN | the enzyme likely plays a central role in the pathway of NAD de novo synthesis in Francisella tularensis | Francisella tularensis | diphosphate + NAD+ | - |
? | |
2.7.7.1 | ATP + NMN | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview | Francisella tularensis | diphosphate + NAD+ | - |
? | |
2.7.7.1 | ATP + NMN | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview | Synechocystis sp. | diphosphate + NAD+ | - |
? | |
3.6.1.13 | ADP-ribose + H2O | - |
Francisella tularensis | AMP + D-ribose 5-phosphate | - |
? | |
3.6.1.13 | ADP-ribose + H2O | - |
Synechocystis sp. | AMP + D-ribose 5-phosphate | - |
? | |
3.6.1.13 | ADP-ribose + H2O | substrate binding structure, overview | Francisella tularensis | AMP + D-ribose 5-phosphate | - |
? | |
3.6.1.13 | ADP-ribose + H2O | substrate binding structure, overview | Synechocystis sp. | AMP + D-ribose 5-phosphate | - |
? | |
3.6.1.13 | additional information | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview | Francisella tularensis | ? | - |
? | |
3.6.1.13 | additional information | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview | Synechocystis sp. | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.7.1 | hexamer | syNadM-Nudix forms hexamer in both crystal and solution with two types of dimer interfaces, the dimer interface is formed primarily through ADPRase domain of each monomer, overview | Synechocystis sp. |
2.7.7.1 | More | bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide adenylyltransferase and an ADP-ribose diphosphatase domain, structures of the N-terminal NadM domain and ADPR domain, overview | Francisella tularensis |
2.7.7.1 | More | bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide adenylyltransferase and an ADP-ribose diphosphatase domain, structures of the N-terminal NadM domain and ADPR domain, overview | Synechocystis sp. |
3.6.1.13 | More | ADPRase Nudix domain of NadM-Nudix and bacterial monofunctional ADPRase are connected by a long alpha helix with ADPRase active site facing away from the NMNATase domain, while the NMNATase active site opens partially toward the ADPRase domain, structure of the ADPRase domain, overview | Francisella tularensis |
3.6.1.13 | More | ADPRase Nudix domain of NadM-Nudix and bacterial monofunctional ADPRase are connected by a long alpha helix with ADPRase active site facing away from the NMNATase domain, while the NMNATase active site opens partially toward the ADPRase domain, structure of the ADPRase domain, overview | Synechocystis sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.1 | More | the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily | Francisella tularensis |
2.7.7.1 | More | the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily | Synechocystis sp. |
2.7.7.1 | NadM-Nudix | - |
Francisella tularensis |
2.7.7.1 | NadM-Nudix | - |
Synechocystis sp. |
2.7.7.1 | NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Francisella tularensis |
2.7.7.1 | NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Synechocystis sp. |
2.7.7.1 | NMNATase | - |
Francisella tularensis |
2.7.7.1 | NMNATase | - |
Synechocystis sp. |
3.6.1.13 | NadM-Nudix | - |
Francisella tularensis |
3.6.1.13 | NadM-Nudix | - |
Synechocystis sp. |
3.6.1.13 | NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Francisella tularensis |
3.6.1.13 | NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Synechocystis sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.6.1.13 | 37 | - |
assay at | Francisella tularensis |
3.6.1.13 | 37 | - |
assay at | Synechocystis sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.1 | 3.6 | - |
ADP-ribose | pH 8.2, 37°C | Francisella tularensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.6.1.13 | 8.2 | - |
assay at | Francisella tularensis |
3.6.1.13 | 8.2 | - |
assay at | Synechocystis sp. |