nicotinate-nucleotide adenylyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.7.18 | ||||||||
CAS no. | 9026-98-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) is an enzyme that catalyzes the chemical reaction
- ATP + nicotinate ribonucleotide diphosphate + deamido-NAD
Thus, the two substrates of this enzyme are ATP and nicotinate ribonucleotide, whereas its two products are diphosphate and deamido-NAD+.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinate-ribonucleotide adenylyltransferase. Other names in common use include deamido-NAD+ pyrophosphorylase, nicotinate mononucleotide adenylyltransferase, deamidonicotinamide adenine dinucleotide pyrophosphorylase, NaMN-ATase, and nicotinic acid mononucleotide adenylyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1K4K, 1K4M, 1KAM, 1KAQ, 1YUL, 1YUM, 1YUN, 2H29, and 2H2A.
References
- Imsande J (May 1961). "Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli". The Journal of Biological Chemistry. 236 (5): 1494–7. doi:10.1016/S0021-9258(18)64203-6. PMID 13717628.
Transferases: phosphorus-containing groups (EC 2.7) | |||||||||||||||
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2.7.1-2.7.4: phosphotransferase/kinase (PO4) |
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2.7.6: diphosphotransferase (P2O7) | |||||||||||||||
2.7.7: nucleotidyltransferase (PO4-nucleoside) |
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2.7.8: miscellaneous |
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2.7.10-2.7.13: protein kinase (PO4; protein acceptor) |
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