Application | Comment | Organism |
---|---|---|
drug development | development of NMNATase inhibitors as potential therapeutics against tularemia | Francisella tularensis |
Crystallization (Comment) | Organism |
---|---|
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. |
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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady state kinetics | Francisella tularensis | |
additional information | - |
additional information | steady state kinetics | Synechocystis sp. | |
0.041 | - |
ADP-ribose | pH 8.2, 37°C | Francisella tularensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + NMN | Synechocystis sp. | the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways | diphosphate + NAD+ | - |
? | |
ATP + NMN | Francisella tularensis | the enzyme likely plays a central role in the pathway of NAD de novo synthesis in Francisella tularensis | diphosphate + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Francisella tularensis | Q5NHR1 | - |
- |
Synechocystis sp. | Q55928 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + nicotinamide ribonucleotide = diphosphate + NAD+ | catalytic mechanism, overview | Francisella tularensis | |
ATP + nicotinamide ribonucleotide = diphosphate + NAD+ | catalytic mechanism, overview | Synechocystis sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + NMN | the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways | Synechocystis sp. | diphosphate + NAD+ | - |
? | |
ATP + NMN | the enzyme likely plays a central role in the pathway of NAD de novo synthesis in Francisella tularensis | Francisella tularensis | diphosphate + NAD+ | - |
? | |
ATP + NMN | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview | Francisella tularensis | diphosphate + NAD+ | - |
? | |
ATP + NMN | the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview | Synechocystis sp. | diphosphate + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
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. |
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 |
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. |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily | Francisella tularensis |
More | the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily | Synechocystis sp. |
NadM-Nudix | - |
Francisella tularensis |
NadM-Nudix | - |
Synechocystis sp. |
NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Francisella tularensis |
NMN adenylyltransferase/ADP-ribose pyrophosphatase | - |
Synechocystis sp. |
NMNATase | - |
Francisella tularensis |
NMNATase | - |
Synechocystis sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.6 | - |
ADP-ribose | pH 8.2, 37°C | Francisella tularensis |