In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme (EC 6.3.2.5) that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:
| Phosphopantothenate—cysteine ligase | |||||||||
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| Identifiers | |||||||||
| EC no. | 6.3.2.5 | ||||||||
| CAS no. | 9023-50-1 | ||||||||
| 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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- NTP + (R)-4'-phosphopantothenate + L-cysteine NMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
The nucleoside triphosphate (NTP) involved in the reaction varies from species to species. Phosphopantothenate—cysteine ligase from the bacterium Escherichia coli uses cytidine triphosphate (CTP) as an energy donor, whilst the human isoform uses adenosine triphosphate (ATP).[1]
Nomenclature
editThis enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide syntheses). The systematic name of this enzyme class is (R)-4'-phosphopantothenate:L-cysteine ligase. This enzyme is also called phosphopantothenoylcysteine synthetase.
Gene
edit| PPCS | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | PPCS, Phosphopantothenate—cysteine ligase, phosphopantothenoylcysteine synthetase, CMD2C | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 609853; MGI: 1915237; HomoloGene: 6173; GeneCards: PPCS; OMA:PPCS - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Phosphopantothenoylcysteine synthetase in humans is encoded by the PPCS gene.[6]
Protein structure
editAs of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1P9O, 1U7U, 1U7W, 1U7Z, and 1U80.
References
edit- ^ Manoj N, Strauss E, Begley TP, Ealick SE (Aug 2003). "Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution". Structure. 11 (8): 927–936. doi:10.1016/S0969-2126(03)00146-1. PMID 12906824.
- ^ a b c GRCh38: Ensembl release 89: ENSG00000127125 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028636 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: Phosphopantothenoylcysteine synthetase".
Further reading
edit- Brown GM (1959). "The metabolism of pantothenic acid". J. Biol. Chem. 234 (2): 370–8. doi:10.1016/S0021-9258(18)70307-4. 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 (17): 13513–6. doi:10.1074/jbc.C100033200. PMID 11278255.
- Kupke T (2002). "Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial dfp flavoproteins". J. Biol. Chem. 277 (39): 36137–45. doi:10.1074/jbc.M206188200. PMID 12140293.
External links
edit- PDBe-KB provides an overview of all the structure information available in the PDB for Human Phosphopantothenate—cysteine ligase
