Supramolecular catalysis of phosphoryl transfer: cocatalysis of pyrophosphate synthesis from acetyl phosphate mediated by macrocyclic polyamines

1987 ◽  
Vol 109 (23) ◽  
pp. 7047-7058 ◽  
Author(s):  
Mir Wais Hosseini ◽  
Jean Marie Lehn

Author(s):  
Hicham Fenniri ◽  
Carol Dallaire ◽  
Daniel P. Funeriu ◽  
Jean-Marie Lehn






2012 ◽  
Vol 11 (10) ◽  
pp. 1249-1256 ◽  
Author(s):  
Matthew L. Fowler ◽  
Cheryl Ingram-Smith ◽  
Kerry S. Smith

ABSTRACTAcetate kinase (ACK) catalyzes the reversible synthesis of acetyl phosphate by transfer of the γ-phosphate of ATP to acetate. Here we report the first biochemical and kinetic characterization of a eukaryotic ACK, that from the protistEntamoeba histolytica. Our characterization revealed that this protist ACK is the only known member of the ASKHA structural superfamily, which includes acetate kinase, hexokinase, and other sugar kinases, to utilize inorganic pyrophosphate (PPi)/inorganic phosphate (Pi) as the sole phosphoryl donor/acceptor. Detection of ACK activity inE. histolyticacell extracts in the direction of acetate/PPiformation but not in the direction of acetyl phosphate/Piformation suggests that the physiological direction of the reaction is toward acetate/PPiproduction. Kinetic parameters determined for each direction of the reaction are consistent with this observation. TheE. histolyticaPPi-forming ACK follows a sequential mechanism, supporting a direct in-line phosphoryl transfer mechanism as previously reported for the well-characterizedMethanosarcina thermophilaATP-dependent ACK. Characterizations of enzyme variants altered in the putative acetate/acetyl phosphate binding pocket suggested that acetyl phosphate binding is not mediated solely through a hydrophobic interaction but also through the phosphoryl group, as for theM. thermophilaACK. However, there are key differences in the roles of certain active site residues between the two enzymes. The absence of known ACK partner enzymes raises the possibility that ACK is part of a novel pathway inEntamoeba.



ChemInform ◽  
1987 ◽  
Vol 18 (22) ◽  
Author(s):  
M. W. HOSSEINI ◽  
J.-M. LEHN ◽  
L. MAGGIORA ◽  
K. B. MERTES ◽  
M. P. MERTES


1989 ◽  
Vol 111 (16) ◽  
pp. 6330-6335 ◽  
Author(s):  
Mir Wais Hosseini ◽  
Jean Marie Lehn ◽  
Kenneth C. Jones ◽  
Kathleen E. Plute ◽  
Kristin Bowman Mertes ◽  
...  


2007 ◽  
Vol 189 (15) ◽  
pp. 5574-5581 ◽  
Author(s):  
Adam H. Klein ◽  
Ana Shulla ◽  
Sylvia A. Reimann ◽  
David H. Keating ◽  
Alan J. Wolfe

ABSTRACT Acetyl phosphate, the intermediate of the AckA-Pta pathway, acts as a global signal in Escherichia coli. Although acetyl phosphate clearly signals through two-component response regulators, it remains unclear whether acetyl phosphate acts as a direct phospho donor or functions through an indirect mechanism. We used two-dimensional thin-layer chromatography to measure the relative concentrations of acetyl phosphate, acetyl coenzyme A, ATP, and GTP over the course of the entire growth curve. We estimated that the intracellular concentration of acetyl phosphate in wild-type cells reaches at least 3 mM, a concentration sufficient to activate two-component response regulators via direct phosphoryl transfer.



ChemInform ◽  
1989 ◽  
Vol 20 (45) ◽  
Author(s):  
M. W. HOSSEINI ◽  
J.-M. LEHN ◽  
K. C. JONES ◽  
K. E. PLUTE ◽  
K. B. MERTES ◽  
...  


1987 ◽  
Vol 109 (2) ◽  
pp. 537-544 ◽  
Author(s):  
Mir Wais Hosseini ◽  
Jean Marie Lehn ◽  
Linda Maggiora ◽  
Kristin B. Mertes ◽  
Mathias P. Mertes


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