Supramolecular catalysis: polyammonium macrocycles as enzyme mimics for phosphoryl transfer in ATP hydrolysis

1989 ◽  
Vol 111 (16) ◽  
pp. 6330-6335 ◽  
Author(s):  
Mir Wais Hosseini ◽  
Jean Marie Lehn ◽  
Kenneth C. Jones ◽  
Kathleen E. Plute ◽  
Kristin Bowman Mertes ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Phosphoryl Transfer ◽  
Enzyme Mimics ◽  
Supramolecular Catalysis

ChemInform Abstract: Supramolecular Catalysis: Polyammonium Macrocycles as Enzyme Mimics for Phosphoryl Transfer in ATP Hydrolysis.

ChemInform ◽  
1989 ◽  
Vol 20 (45) ◽  
Author(s):  
M. W. HOSSEINI ◽  
J.-M. LEHN ◽  
K. C. JONES ◽  
K. E. PLUTE ◽  
K. B. MERTES ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Phosphoryl Transfer ◽  
Enzyme Mimics ◽  
Supramolecular Catalysis

scholarly journals Supramolecular catalysis. Part 2: artificial enzyme mimics

2014 ◽  
Vol 43 (5) ◽  
pp. 1734-1787 ◽  
Author(s):  
Matthieu Raynal ◽  
Pablo Ballester ◽  
Anton Vidal-Ferran ◽  
Piet W. N. M. van Leeuwen
Keyword(s):  
Enzyme Mimics ◽  
Artificial Enzyme ◽  
Supramolecular Catalysis

Supramolecular catalysis beyond enzyme mimics

2010 ◽  
Vol 2 (8) ◽  
pp. 615-621 ◽  
Author(s):  
Jurjen Meeuwissen ◽  
Joost N. H. Reek
Keyword(s):  
Enzyme Mimics ◽  
Supramolecular Catalysis

ChemInform Abstract: Supramolecular Catalysis. Part 2. Artificial Enzyme Mimics

ChemInform ◽  
2014 ◽  
Vol 45 (20) ◽  
pp. no-no
Author(s):  
Matthieu Raynal ◽  
Pablo Ballester ◽  
Anton Vidal-Ferran ◽  
Piet W. N. M. van Leeuwen
Keyword(s):  
Enzyme Mimics ◽  
Artificial Enzyme ◽  
Supramolecular Catalysis

scholarly journals Effects of phospholipid fatty acyl chain length on phosphorylation and dephosphorylation of the Ca2+-ATPase

1995 ◽  
Vol 310 (3) ◽  
pp. 875-879 ◽  
Author(s):  
A P Starling ◽  
J M East ◽  
A G Lee
Keyword(s):  
Atp Hydrolysis ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Phosphoryl Transfer ◽  
Acyl Chain Length ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting ◽  
Kinetics Of

The kinetics of the Ca(2+)-ATPase purified from sarcoplasmic reticulum have been studied after reconstitution into bilayers of dimyristoleoylphosphatidylcholine [di(C14:1)PC], dioleoylphosphatidylcholine[di(C18:1)PC] and dinervonylphosphatidylcholine [di(C24:1)PC]. In di(C24:1)PC the rate of phosphorylation of the ATPase by ATP was comparable with that in di(C18:1)PC (about 70 s-1), but in di(C14:1)PC the rate was much lower (21 s-1). Fluorescence responses of the ATPase suggest changes in the phosphoryl-transfer step rather than in the preceding conformational change E1Ca2ATP<-->E1′Ca2ATP. The rate of dephosphorylation of the phosphorylated ATPase was found to decrease in the order di(C24:1)PC < di(C14:1)PC < di(C18:1)PC. For the ATPase in di(C24:1)PC the rate of dephosphorylation (3.3 s-1) was slow enough to be the rate-limiting step for ATP hydrolysis; in di(C14:1)PC, it is suggested that both phosphorylation and dephosphorylation contribute to rate limitation. Phosphorylation of the ATPase in di(C24:1)PC by Pi was normal, but no phosphoenzyme could be detected in di(C14:1)PC. The rate of the Ca(2+)-transport step was normal in di(C24:1)PC, suggesting that the single Ca2+ ion bound to the ATPase in di(C24:1)PC could be transported.

scholarly journals Mapping Free Energy Pathways for ATP Hydrolysis in the E. coli ABC Transporter HlyB by the String Method

Molecules ◽  
2018 ◽  
Vol 23 (10) ◽  
pp. 2652 ◽  
Author(s):  
Yan Zhou ◽  
Pedro Ojeda-May ◽  
Mulpuri Nagaraju ◽  
Bryant Kim ◽  
Jingzhi Pu
Keyword(s):  
Free Energy ◽  
Abc Transporter ◽  
Atp Hydrolysis ◽  
Minimum Free Energy ◽  
Phosphoryl Transfer ◽  
String Method ◽  
Collective Variables ◽  
E Coli ◽  
Energy Profiles ◽  
Proton Relay

HlyB functions as an adenosine triphosphate (ATP)-binding cassette (ABC) transporter that enables bacteria to secrete toxins at the expense of ATP hydrolysis. Our previous work, based on potential energy profiles from combined quantum mechanical and molecular mechanical (QM/MM) calculations, has suggested that the highly conserved H-loop His residue H662 in the nucleotide binding domain (NBD) of E. coli HlyB may catalyze the hydrolysis of ATP through proton relay. To further test this hypothesis when entropic contributions are taken into account, we obtained QM/MM minimum free energy paths (MFEPs) for the HlyB reaction, making use of the string method in collective variables. The free energy profiles along the MFEPs confirm the direct participation of H662 in catalysis. The MFEP simulations of HlyB also reveal an intimate coupling between the chemical steps and a local protein conformational change involving the signature-loop residue S607, which may serve a catalytic role similar to an Arg-finger motif in many ATPases and GTPases in stabilizing the phosphoryl-transfer transition state.

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