phosphopantetheinyltransferase
holo-[acyl-carrier-protein] synthase trimer, Helicobacter pylori
Identifiers
EC no.	2.7.8.7
CAS no.	37278-30-1
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
Search PMC articles PubMed articles NCBI proteins

ACPS
crystal structure of the 4'-phosphopantetheinyl transferase sfp-coenzyme a complex
Identifiers
Symbol	ACPS
Pfam	PF01648
InterPro	IPR008278
SCOP2	1qr0 / SCOPe / SUPFAM
Available protein structures: PDB   IPR008278 PF01648 (ECOD; PDBsum)   AlphaFold IPR008278 PF01648

In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase (ACPS, EC 2.7.8.7) is an enzyme that catalyzes the chemical reaction:

Contents

• Function
• Nomenclature
• Structural studies
• References
• Further reading

CoA-[4'-phosphopantetheine] + apo-acyl carrier protein ${\displaystyle \rightleftharpoons }$ adenosine 3',5'-bisphosphate + holo-acyl carrier protein

This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups, and more specifically to the 4'-phosphopantetheinyl transferases (PPTases) named after the group they transfer.

In mammals, this activity is performed by the PPTase, aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASDHPPT), which acts in both the cytosol and mitochondria and also modifies non-acyl carrier protein (ACP) substrates. ^[1]

Function

All ACPS enzymes known so far are evolutionally related to each other in a single superfamily of proteins. It transfers a 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to an invariant serine in an acyl carrier protein (ACP), a small protein responsible for acyl group activation in fatty acid biosynthesis. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. ^[2] This superfamily consists of two subtypes: the trimeric ACPS type such as E. coli ACPS and the monomeric Sfp (PCP-synthesizing) type such as B. subtilis SFP. Structures from both families are now known. The active site accommodates a magnesium ion. The most highly conserved regions of the protein are involved in binding the magnesium ion. ^{[3] [4]}

Nomenclature

The systematic name of this enzyme class is CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein] 4'-pantetheinephosphotransferase. Other names in common use, disregarding the synthetase/synthase spelling difference, include acyl carrier protein holoprotein synthetase, holo-ACP synthetase, coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine, acyl carrier protein synthetase (ACPS), PPTase, acyl carrier protein synthase, P-pant transferase, and CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase.^{[ citation needed ]}

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1F7L, 1F7T, 1F80, 1FTE, 1FTF, 1FTH, 2JBZ, and 2JCA.

References

Further reading

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