6.3.5.1: NAD+ synthase (glutamine-hydrolysing)

This is an abbreviated version!
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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Results	in table
2	Activating Compound
29511	AA Sequence
2	Application
1	CAS Registry Number
10	Cloned(Commentary)
3	Cofactor
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
12	Pathway
44	PDB ID
8	pH Optimum
2	pH Range
1	pH Stability
30	Protein Variants
10	Purification (Commentary)
1	Reaction
1	Reaction Type
21	Reference
19	Source Tissue
25	Specific Activity [micromol/min/mg]
2	Storage Stability
35	Substrates and Products (Substrate)
7	Subunits
36	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
21	Turnover Number [1/s]

Engineering

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

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

S740I

2 entries

C175S

Homo sapiens

Q6IA69

in contrast with the wild-type NADsyn1, the activity of the mutant NADsyn1 (C175S-NADsyn1) is not detected when glutamine is used as a substrate, whereas the activity remains unaltered with NH4Cl

652364

C176A

3 entries

D656A

Mycobacterium tuberculosis

-

strong decrease in catalytic efficiency

705873

E52A

Mycobacterium tuberculosis

-

complete loss of glutamine-dependent activity, retains 30% of its NH3-dependent activity

663373

K121A

Mycobacterium tuberculosis

-

complete loss of glutamine-dependent and NH3-dependent activity

663373

L486A

Mycobacterium tuberculosis

P9WJJ3

site-directed mutagenesis

726904

L486F

Mycobacterium tuberculosis

P9WJJ3

site-directed mutagenesis

726904

Y58A

Mycobacterium tuberculosis

P9WJJ3

site-directed mutagenesis

726904

C176A

Mycobacterium tuberculosis H37Rv

-

site-directed mutagenesis, inactive mutant, analysis of ligand binding structures

-

L486A

Mycobacterium tuberculosis H37Rv

-

site-directed mutagenesis

-

L486F

Mycobacterium tuberculosis H37Rv

-

site-directed mutagenesis

-

Y58A

Mycobacterium tuberculosis H37Rv

-

site-directed mutagenesis

-

D593A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

D593A/F622A

Saccharomyces cerevisiae

-

synthetase dead

674687

E177A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

F622A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

I111A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

L529A/L604A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

L604A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

L604N

Saccharomyces cerevisiae

-

poor synthetase activity

674687

M621A

Saccharomyces cerevisiae

-

synthetase mutant that depresses all activities

674687

R112L

Saccharomyces cerevisiae

-

poor synthetase activity that inhibit substrate synergism

674687

R112S

Saccharomyces cerevisiae

-

poor synthetase activity that inhibit substrate synergism

674687

Y532A/Y601A

Saccharomyces cerevisiae

-

synthetase dead

674687

Y601A

Saccharomyces cerevisiae

-

poor synthetase activity

674687

Y601A/M621A

Saccharomyces cerevisiae

-

synthetase dead

674687

S740I

Chlamydomonas reinhardtii

C4PG67

Chlamydomonas cells bearing a NAD+ synthase mutation have a defective NAD+ de novo synthesis pathway. Mutant cells show longer vegitative life span than wild-type cells. Up-regulation of a sirtuin gene is linked to the extended life span in the mutant strain

716662

S740I

Chlamydomonas reinhardtii

C4PG67

mutant fails to grow on Sager and Granick rich medium without nicotinamide or Sager and Garnick medium supplemented with 3-acetylpyridine. Mutants grows well on media supplied with either nicotinamide or NMN. Addition of nicotinic acid shows very weak rescue of the nic- mutant phenotype. Addition of 3-hydroxyanthranilate cannot rescue the growth defect. Sirtuin SRT2 levels are 2- to 2.5fold increased in the mutant with concomitant increase in reproductive capactiy

716662

C176A

Mycobacterium tuberculosis

-

complete loss of glutamine-dependent activity, retains 90% of its NH3-dependent activity

663373

C176A

Mycobacterium tuberculosis

-

activity smilar to wild-type

705873

C176A

Mycobacterium tuberculosis

P9WJJ3

site-directed mutagenesis, inactive mutant, analysis of ligand binding structures

726904