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EC Tree
IUBMB Comments NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase).
The taxonomic range for the selected organisms is: Homo sapiens The enzyme appears in selected viruses and cellular organisms
Synonyms
nade1, nitrogen-regulatory protein, glutamine-dependent nad synthetase, mtunade, glutamine-dependent nad+ synthetase, gsp38, glutamine-dependent nadegln, nicotinamide adenine dinucleotide synthetase enzyme,
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General stress protein 38
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NAD synthetase (glutamine)
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NAD(+) synthase [glutamine-hydrolyzing]
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NAD+ synthetase (glutamine-hydrolysing)
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Nicotinamide adenine dinucleotide synthetase (glutamine)
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Nitrogen-regulatory protein
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Sporulation protein outB
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Synthetase, nicotinamide adenine dinucleotide (glutamine)
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deamido-NAD+:L-glutamine amido-ligase (AMP-forming)
NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase).
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ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
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ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
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ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
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ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
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K+
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required
Mg2+
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required
Mg2+
required for activity
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Tuberculosis
Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain.
Tuberculosis
Regulation of the inter subunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase.
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1.44
L-glutamine
37°C, wild-type NADsyn1
0.015
ATP
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pH 7.5
0.089
ATP
37°C, wild-type NADsyn1
0.12
ATP
37°C, NADsyn1 C175S mutant
0.04
deamido-NAD+
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pH 7.5
0.049
deamido-NAD+
37°C, wild-type NADsyn1
0.2
deamido-NAD+
37°C, NADsyn1 C175S mutant
13.1
NH3
37°C, wild-type NADsyn1
23.9
NH3
37°C, NADsyn1 C175S mutant
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additional information
additional information
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additional information
additional information
the Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
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additional information
additional information
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the Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
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additional information
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coupled enzyme assay for the measurement of recombinant human NAD+ synthetase by employing lactate dehydrogenase in a cycling/amplification reaction linked ultimately to the fluorescence generation of resorufin from reazurin via diaphorase
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6 - 8
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6.0: about 75% of maximal activity, 8.0: about 55% of maximal activity
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SwissProt
brenda
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the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
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brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
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NADE_HUMAN
706
0
79285
Swiss-Prot
other Location (Reliability: 5 )
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500000
non-denaturing PAGE
80000
6 * 80000, wild-type and C175S mutant enzyme, SDS-PAGE
80300
6 * 80300, calculated from sequence
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hexamer
6 * 80000, wild-type and C175S mutant enzyme, SDS-PAGE
hexamer
6 * 80300, calculated from sequence
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C175S
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
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EDTA and KCl increase stability substantially
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4°C, 24 h, complete loss of activity
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expression in Sf9 insect cells
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expression of Nadsyn1 and mutant enzyme C175S as His6-tagged proteins in COS-7 cells
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medicine
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erythrocyte NAD synthetase is activated by lead, and the activity is a sensitive indicator of lead exposure in human
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Zerez, C.R.; Wong, M.D.; Tanaka, K.R.
Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure
Blood
75
1576-1582
1990
Homo sapiens
brenda
Hara, N.; Yamada, K.; Terashima, M.; Osago, H.; Shimoyama, M.; Tsuchiya, M.
Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency
J. Biol. Chem.
278
10914-10921
2003
Homo sapiens (Q6IA69), Homo sapiens
brenda
Bembenek, M.E.; Kuhn, E.; Mallender, W.D.; Pullen, L.; Li, P.; Parsons, T.
A fluorescence-based coupling reaction for monitoring the activity of recombinant human NAD synthetase
Assay Drug Dev. Technol.
3
533-541
2005
Homo sapiens
brenda