| Pantoate—β-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.1 | ||||||||
| CAS no. | 9023-49-8 | ||||||||
| 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 | ||||||||
| |||||||||
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 1IHO, 1MOP, 1N2B, 1N2E, 1N2G, 1N2H, 1N2I, 1N2J, 1N2O, 1UFV, 1V8F, 2A7X, 2A84, 2A86, and 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. PMID 12999714.
- Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305–306.
| Pantoate—β-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.1 | ||||||||
| CAS no. | 9023-49-8 | ||||||||
| 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 | ||||||||
| |||||||||
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 1IHO, 1MOP, 1N2B, 1N2E, 1N2G, 1N2H, 1N2I, 1N2J, 1N2O, 1UFV, 1V8F, 2A7X, 2A84, 2A86, and 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. PMID 12999714.
- Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305–306.