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.
Word Map on EC 6.3.5.1
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6.3.5.1
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ammonia
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synthetases
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nicotinic
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typhimurium
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nitrilase
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glutaminase
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ammonia-dependent
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nitrogen-limiting
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enhancer-binding
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tuberculosis
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nh3-dependent
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salvage
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adenylyltransferase
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amidotransferase
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synthesis
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medicine
- 6.3.5.1
- ammonia
- synthetases
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nicotinic
- typhimurium
- nitrilase
- glutaminase
-
ammonia-dependent
-
nitrogen-limiting
-
enhancer-binding
- tuberculosis
-
nh3-dependent
-
salvage
- adenylyltransferase
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amidotransferase
- synthesis
- medicine
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)
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General Information
General Information on EC 6.3.5.1 - NAD+ synthase (glutamine-hydrolysing)
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evolution
malfunction
metabolism
due to the presence of an additional glutamine transferase domain, abNadE can efficiently utilize l-glutamine (as well as ammonia) for the amidation of NAD precursor
physiological function
nadE, encoding glutamine-dependent NAD synthetase, is dispensable when the nondeamidating salvage pathway of nicotinamide salvage/recycling functions as the only route of NAD biogenesis
additional information
most residues lining the ATP-binding site are conserved among the glutamine-dependent NAD+ synthetases, whereas residues not conserved, such as Leu399 andGly366, interact with the adenine ring and the adenylyl ribose with the backbone oxygen and nitrogen
evolution
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most residues lining the ATP-binding site are conserved among the glutamine-dependent NAD+ synthetases, whereas residues not conserved, such as Leu399 andGly366, interact with the adenine ring and the adenylyl ribose with the backbone oxygen and nitrogen
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a homolog of the human SIRT6-like gene, SRT2, is upregulated in the NAD+ synthase mutant, which shows a longer vegetative life span than wild-type cells
malfunction
nadE is dispensable when the nondeamidating salvage pathway functions as the only route of NAD biogenesis
the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
additional information
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the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
additional information
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the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
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