Pantoate—beta-alanine ligase
| Pantoate—β-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.1 | ||||||||
| CAS no. | 9023-49-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a pantoate—β-alanine ligase (EC 6.3.2.1) is an enzyme that catalyzes the chemical reaction
- ATP + (R)-pantoate + β-alanine AMP + diphosphate + (R)-pantothenate
The 3 substrates of this enzyme are ATP, (R)-pantoate, and beta-alanine, whereas its 3 products are AMP, diphosphate, and (R)-pantothenate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is (R)-pantoate:beta-alanine ligase (AMP-forming). Other names in common use include pantothenate synthetase, pantoate activating enzyme, pantoic-activating enzyme, and D-pantoate:beta-alanine ligase (AMP-forming). This enzyme participates in beta-alanine metabolism and pantothenate and CoA biosynthesis.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1IHO, PDB: 1MOP, PDB: 1N2B, PDB: 1N2E, PDB: 1N2G, PDB: 1N2H, PDB: 1N2I, PDB: 1N2J, PDB: 1N2O, PDB: 1UFV, PDB: 1V8F, PDB: 2A7X, PDB: 2A84, PDB: 2A86, and PDB: 2A88.
References
- GINOZA HS, ALTENBERN RA (1955). "The pantothenate-synthesizing enzyme in cell-free extracts of Brucella abortus, strain 19". Arch. Biochem. 56 (2): 537–41. doi:10.1016/0003-9861(55)90273-3. PMID 14377603.
- MAAS WK (1952). "Pantothenate studies. III. Description of the extracted pantothenate-synthesizing enzyme of Escherichia coli". J. Biol. Chem. 198 (1): 23–32. doi:10.1016/S0021-9258(18)55553-8. PMID 12999714.
- Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305–306.