Rahul Sharma (Editor)

Phosphopantothenate—cysteine ligase

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EC number
  
6.3.2.5

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
9023-50-1

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

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:

Contents

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).

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

Phosphopantothenoylcysteine synthetase in humans is encoded by the PPCS gene.

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

Phosphopantothenate—cysteine ligase Wikipedia