EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Mus musculus |
nicotinate-adenine dinucleotide phosphate |
- |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Oryctolagus cuniculus |
nicotinate-adenine dinucleotide phosphate |
- |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Homo sapiens |
nicotinate-adenine dinucleotide phosphate |
- |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Rattus norvegicus |
nicotinate-adenine dinucleotide phosphate |
- |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Aplysia californica |
nicotinate-adenine dinucleotide phosphate |
- |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Aplysia californica |
nicotinate-adenine dinucleotide phosphate |
enzyme shows a higher NAADP+-producing activity at pH 5.0 than at pH 7.4. At pH 5.0 the formation of NAADP+ is even more predominant than cADPRP hydrolysis, reaction of EC 3.2.2.6 |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Axinella polypoides |
nicotinate-adenine dinucleotide phosphate |
enzyme shows a higher NAADP+-producing activity at pH 5.0 than at pH 7.4. At pH 5.0 the formation of NAADP+ is even more predominant than cADPRP hydrolysis, reaction of EC 3.2.2.6 |
? |
2.4.99.20 | 2'-phospho-cyclic ADP-ribose + nicotinate |
- |
Homo sapiens |
nicotinate-adenine dinucleotide phosphate |
the synthesis of nicotinate-adenine dinucleotide phosphate from 2'-phospho-cyclic ADP-ribose is as efficient as the hydrolysis of the cyclic nucleotide at pH 5.0, reaction of EC 3.2.2.6, while at pH 7.4 the hydrolase activity is predominant |
? |
2.4.99.20 | more |
enzyme is more efficient in catalyzing the removal of the nicotinamide moiety than in the base-exchange reaction |
Homo sapiens |
? |
- |
? |
2.4.99.20 | more |
enzyme is more efficient in catalyzing the removal of the nicotinamide moiety than in the base-exchange reaction |
Aplysia californica |
? |
- |
? |