Phosphopantothenate-cysteine ligase

From Wikipedia, the free encyclopedia

In enzymology, a phosphopantothenate-cysteine ligase (EC 6.3.2.5) is an enzyme that catalyzes the chemical reaction

CTP + (R)-4'-phosphopantothenate + L-cysteine $\rightleftharpoons$ CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine

The 3 substrates of this enzyme are CTP, (R)-4'-phosphopantothenate, and L-cysteine, whereas its 3 products are CMP, diphosphate, and [[N-[(R)-4'-phosphopantothenoyl]-L-cysteine]].

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)-4'-phosphopantothenate:L-cysteine ligase. This enzyme is also called phosphopantothenoylcysteine synthetase. This enzyme participates in 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, 5 structures have been solved for this class of enzymes, with PDB accession codes 1P9O, 1U7U, 1U7W, 1U7Z, and 1U80.

[edit] References

IUBMB entry for 6.3.2.5
BRENDA references for 6.3.2.5 (Recommended.)
PubMed references for 6.3.2.5
PubMed Central references for 6.3.2.5
Google Scholar references for 6.3.2.5
BROWN GM (1959). "The metabolism of pantothenic acid". J. Biol. Chem. 234: 370–8. PMID 13630913.
Strauss E, Kinsland C, Ge Y, McLafferty FW, Begley TP (2001). "Phosphopantothenoylcysteine synthetase from Escherichia coli Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria". J. Biol. Chem. 276: 13513–6. PMID 11278255.
Kupke T (2002). "Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial dfp flavoproteins". J. Biol. Chem. 277: 36137–45. doi:10.1074/jbc.M206188200. PMID 12140293.