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adenosine triphosphopyridoxal

Known as: AP3-PL 
 
National Institutes of Health

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Adenosine Triphosphate
analogs & derivatives

Papers overview

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1994
1994
Catalysis and energy coupling of H(+)-ATPase (ATP synthase): molecular biological approaches.
The molecular biological approach has provided important information for understanding the F0F1 H(+)-ATPase. This article focuses… Expand
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1993
1993
Use of adenosine (5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B.
Adenosine(5')polyphospho(5')pyridoxals (APn-PLs, n = 2, 3, 4) were examined for affinity labeling of glutathione synthetase (EC 6… Expand
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Review
1992
Review
1992
Escherichia coli F0F1-ATPase. Residues involved in catalysis and coupling.
The molecular biological approach has provided important information toward understanding the complexities of the F0F1 ATPase… Expand
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1991
1991
Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.
The catalytic site of Escherichia coli F1 was probed using a reactive ATP analogue, adenosine triphosphopyridoxal (AP3-PL). For… Expand
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1990
1990
Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl-and valyl…
Pyridoxal 5'-triphospho-5'-adenosine (AP3-PL), the affinity labeling reagent specific for lysine residues in the nucleotide… Expand
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1988
1988
The ATP-binding site in gamma subunit of phosphorylase kinase.
To reveal the structure of the ATP-binding site(s) in rabbit muscle phosphorylase kinase, we modified the enzyme with adenosine… Expand
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1987
1987
Loss of unisite and multisite catalyses by Escherichia coli F1 through modification with adenosine tri- or tetraphosphopyridoxal.
Pyridoxal phosphate (PLP) and adenosine diphospho (AP2-PL)-, triphospho (AP3-PL)-, and tetraphospho (AP4-PL)-pyridoxals (Tagaya… Expand
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