Phosphopantothenate—cysteine ligase explained

Phosphopantothenate—cysteine ligase
Ec Number:6.3.2.5
Cas Number:9023-50-1
Go Code:0004632

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

\rightleftharpoons

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 syntheses). The systematic name of this enzyme class is (R)-4'-phosphopantothenate:L-cysteine ligase. This enzyme is also called phosphopantothenoylcysteine synthetase.

Gene

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,,,, and .

Further reading

External links

Notes and References

  1. 10.1016/S0969-2126(03)00146-1 . Structure . Aug 2003 . 11. 8 . 927–936 . Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution . Manoj N, Strauss E, Begley TP, Ealick SE . 12906824. free .
  2. Web site: Entrez Gene: Phosphopantothenoylcysteine synthetase .