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Literature summary for 2.7.7.1 extracted from

  • Huang, N.; Sorci, L.; Zhang, X.; Brautigam, C.A.; Li, X.; Raffaelli, N.; Magni, G.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
    Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism (2008), Structure, 16, 196-209.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.1

Application

Application Comment Organism
drug development development of NMNATase inhibitors as potential therapeutics against tularemia Francisella tularensis

Crystallization (Commentary)

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Francisella tularensis Q5NHR1
-
-
Synechocystis sp. Q55928
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + nicotinamide ribonucleotide = diphosphate + NAD+ catalytic mechanism, overview Francisella tularensis
a
ATP + nicotinamide ribonucleotide = diphosphate + NAD+ catalytic mechanism, overview Synechocystis sp.
a

Substrates and Products (Substrate)

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

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

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 [1/s]

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