Literature summary for 2.7.8.7 extracted from

Dallaglio, P.; Arthur, C.J.; Williams, C.; Vasilakis, K.; Maple, H.J.; Crosby, J.; Crump, M.P.; Hadfield, A.T.
Analysis of Streptomyces coelicolor phosphopantetheinyl transferase, AcpS, reveals the basis for relaxed substrate specificity (2011), Biochemistry, 50, 5704-5717.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment)	Organism
complexed with CoA and acetyl-CoA, and mutant enzymes H110A and D111A, vapor diffusion method. Crystals of the AcpS-CoA-Mg2+ complex are obtained at 18°C, from 0.3 M potassium thiocyanate (KSCN), 0.1 M sodium cacodylate (NaCac) (pH 6.5), and 15% (w/v) PEG 4000. The best diffracting crystal of the AcpS-acetyl-CoA complex is obtained in 0.2 M lithium sulfate, 25% (w/v) PEG 2000 MME, and 0.1 M NaCac (pH 6.5), in the presence of 5 mM acetyl-CoA. The D111A mutant crystallizes in 0.2 M KSCN, 0.1 M NaCac (pH 6.5), 8% (w/v) PEG 20000, and 8% (w/v) PEG 550 MME. The H110A mutant crystal is obtained in 0.3 Ms odium acetate, 0.1 M NaCac (pH 6.5), and 25% (w/v) PEG 2000 MME	Streptomyces coelicolor

Crystallization (Comment)

Organism

complexed with CoA and acetyl-CoA, and mutant enzymes H110A and D111A, vapor diffusion method. Crystals of the AcpS-CoA-Mg2+ complex are obtained at 18°C, from 0.3 M potassium thiocyanate (KSCN), 0.1 M sodium cacodylate (NaCac) (pH 6.5), and 15% (w/v) PEG 4000. The best diffracting crystal of the AcpS-acetyl-CoA complex is obtained in 0.2 M lithium sulfate, 25% (w/v) PEG 2000 MME, and 0.1 M NaCac (pH 6.5), in the presence of 5 mM acetyl-CoA. The D111A mutant crystallizes in 0.2 M KSCN, 0.1 M NaCac (pH 6.5), 8% (w/v) PEG 20000, and 8% (w/v) PEG 550 MME. The H110A mutant crystal is obtained in 0.3 Ms odium acetate, 0.1 M NaCac (pH 6.5), and 25% (w/v) PEG 2000 MME

Streptomyces coelicolor

Protein Variants

Protein Variants	Comment	Organism
D111A	active site mutant exhibiting 5% of wild type activity	Streptomyces coelicolor
E57A	active site mutant without any activity	Streptomyces coelicolor
H110A	active site mutant exhibiting 28% of wild type activity	Streptomyces coelicolor
R15A	active site mutant exhibiting 15% of wild type activity	Streptomyces coelicolor

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	contains Mg2+	Streptomyces coelicolor

Organism

Organism	UniProt	Comment	Textmining
Streptomyces coelicolor	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni2+ affinity column chromatography and Superdex 75 gel filtration	Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetyl-CoA + apo-[acyl-carrier protein]	-	Streptomyces coelicolor	CoA + acetyl-[acyl-carrier protein]	-	?
CoA + apo-[acyl-carrier protein]	-	Streptomyces coelicolor	adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]	-	?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]	-	Streptomyces coelicolor	adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]	-	?

Subunits

Subunits	Comment	Organism
trimer	x-ray crystallography	Streptomyces coelicolor

Synonyms

Synonyms	Comment	Organism
AcpS	-	Streptomyces coelicolor
phosphopantetheinyl transferase	-	Streptomyces coelicolor
PPTase	-	Streptomyces coelicolor

Cofactor

Cofactor	Comment	Organism	Structure
4'-phosphopantetheine	-	Streptomyces coelicolor

General Information

General Information	Comment	Organism
metabolism	AcpS is a doubly promiscuous enzyme capable of activation of acyl-carrier proteins from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates	Streptomyces coelicolor