Phosphopantothenate—cysteine ligase

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phosphopantothenate-cysteine ligase
Identifiers
EC number6.3.2.5
CAS number9023-50-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a phosphopantothenate-cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:

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

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.

Gene

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Phosphopantothenoylcysteine synthetase in humans is encoded by the PPCS gene.[2]

Protein structure

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1P9O, 1U7U, 1U7W, 1U7Z, and 1U80.

References

  1. 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.
  2. "Entrez Gene: Phosphopantothenoylcysteine synthetase".

Further reading

  • Brown GM (1959). "The metabolism of pantothenic acid". J. Biol. Chem. 234 (2): 370&ndash, 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 (17): 13513&ndash, 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&ndash, 45. doi:10.1074/jbc.M206188200. PMID 12140293.

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