Pantoate-beta-alanine ligase

From Wikipedia, the free encyclopedia

In enzymology, a pantoate-beta-alanine ligase (EC 6.3.2.1) is an enzyme that catalyzes the chemical reaction

ATP + (R)-pantoate + beta-alanine $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 6.3.2.1
BRENDA references for 6.3.2.1 (Recommended.)
PubMed references for 6.3.2.1
PubMed Central references for 6.3.2.1
Google Scholar references for 6.3.2.1
GINOZA HS, ALTENBERN RA (1955). "The pantothenate-synthesizing enzyme in cell-free extracts of Brucella abortus, strain 19". Arch. Biochem. 56: 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: 23–32. PMID 12999714.
Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305–306.