6.3.1.5: NAD+ synthase
This is an abbreviated version!
For detailed information about NAD+ synthase, go to the full flat file.
Word Map on EC 6.3.1.5
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6.3.1.5
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adenylyltransferase
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nmnat
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glutamine-dependent
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nucleolus-associated
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analysis
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pharmacology
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drug development
- 6.3.1.5
- adenylyltransferase
- nmnat
-
glutamine-dependent
-
nucleolus-associated
- analysis
- pharmacology
- drug development
Reaction
Synonyms
ammonia-dependent NADS, ammonia-dependent nicotinamide adenine dinucleotide synthetase, ammonia-specific NAD synthase, ammonia-specific NAD synthetase, Diphosphopyridine nucleotide synthetase, draNADS, MJ1352, mj_NADS, NAD synthase, NAD synthetase, NAD+ synthetase, NadE, NADS, NH3-dependent NAD+ synthetase, Nicotinamide adenine dinucleotide synthetase, Qns1, Synthetase, nicotinamide adenine dinucleotide
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Metals Ions
Metals Ions on EC 6.3.1.5 - NAD+ synthase
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K+
required, 2 binding sites near the bound diphosphate at the ATP-binding site, can be substituted by Tl+
Mg2+
Mn2+
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can satisfy the metal ion requirement, Mn2+ is more effective than Mg2+ at low concentrations, at high concentrations Mn2+ markedly inhibits, but Mg2+ does not
Mg2+
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required, binding structure and mechanism, 2 binding sites per molecule of enzyme
Mg2+
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can satisfy the metal ion requirement, Mn2+ is more effective than Mg2+ at low concentrations, at high concentrations Mn2+ markedly inhibits, but Mg2+ does not