Pantetheine-phosphate adenylyltransferase

In enzymology, a pantetheine-phosphate adenylyltransferase (EC 2.7.7.3) is an enzyme that catalyzes the chemical reaction

ATP + 4'-Phosphopantetheine${\displaystyle \rightleftharpoons }$ diphosphate + 3'-dephospho-CoA

pantetheine-phosphate adenylyltransferase
Phosphopantetheine adenylyltransferase from Thermotoga maritima. 4'-Phosphopantetheine shown as spheres. PDB 1vlh
Identifiers
EC no.	2.7.7.3
CAS no.	9026-99-7
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
Search PMC articles PubMed articles NCBI proteins

Thus, the two substrates of this enzyme are ATP and 4'-Phosphopantetheine, whereas its two products are diphosphate and 3'-dephospho-CoA.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:pantetheine-4'-phosphate adenylyltransferase. Other names in common use include dephospho-CoA pyrophosphorylase, pantetheine phosphate adenylyltransferase, dephospho-coenzyme A pyrophosphorylase, and 3'-dephospho-CoA pyrophosphorylase. This enzyme participates in pantothenate and coa biosynthesis.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1B6T, 1GN8, 1H1T, 1O6B, 1OD6, 1QJC, 1TFU, and 1VLH.