6.3.5.1: NAD+ synthase (glutamine-hydrolysing)

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For detailed information about NAD+ synthase (glutamine-hydrolysing), go to the full flat file.

Reaction

Synonyms

abNadE, General stress protein 38, glutamine-dependent NAD synthetase, glutamine-dependent NAD+ synthetase, glutamine-dependent NadEGln, GSP38, Hsero_1894, mtuNadE, NAD synthetase (glutamine), NAD(+) synthase [glutamine-hydrolyzing], NAD+ synthase, NAD+ synthetase, NAD+ synthetase (glutamine-hydrolysing), NadE-679, NadE-738, NadE1, NADS, nic13, Nicotinamide adenine dinucleotide synthetase (glutamine), nicotinamide adenine dinucleotide synthetase enzyme, Nitrogen-regulatory protein, Qns1, Sporulation protein outB, Synthetase, nicotinamide adenine dinucleotide (glutamine)

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor

                6.3.5.1 NAD+ synthase (glutamine-hydrolysing)

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2	Activating Compound
29511	AA Sequence
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2	Crystallization (Commentary)
5	Disease/ Diagnostics
8	General Information
2	General Stability
4	IC50 Value
15	Inhibitors
18	kcat/KM [mM/s]
1	Ki Value [mM]
65	KM Value [mM]
12	Metals/Ions
11	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
22	Organism
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44	PDB ID
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21	Reference
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25	Specific Activity [micromol/min/mg]
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35	Substrates and Products (Substrate)
7	Subunits
36	Synonyms
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1	Temperature Range [°C]
21	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.3.5.1 - NAD+ synthase (glutamine-hydrolysing)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

native enzyme and selenomethionine-derivative, to 2.35 and 3.0 A resolution, respectively. Homooctameric subunit organization suggesting a tight dependence of catalysis on the quaternary structure, a 40 A intersubunit ammonia tunnel and structural elements that may be involved in the transfer of information between catalytic sites

Mycobacterium tuberculosis

-

705873

wild-type mtuNadE in complex with 6-diazo-5-oxo-L-norleucine/NaAD+ and mutant enzymes, hanging drop vapour diffusion method, different combinations of the ligands 3 mM NaAD+, 4 mM ATP, 7 mM adenosine 5'-[alpha,beta-methylene]triphosphate, 20 mM L-glutamine, 6 mM NAD+, 10 mM AMP, 4 mM diphosphate, 100 mM L-glutamate, and 10 mM or 120 mM MgCl2 are used in the co-crystallization experiments, crystallization solution contains 1.2-1.6 M ammonium citrate tribasic, pH 6.5-8.0, with 5-15% v/v glycerol, 20°C, X-ray diffraction structure determination analysis at 2.0-2.85 A resolution, molecular replacement

Mycobacterium tuberculosis

P9WJJ3

726904