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adenosine triphosphopyridoxal

Known as: AP3-PL 
 
National Institutes of Health

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2 relations

Broader (1)

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
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
Review
1992
Review
1992
Escherichia coli F0F1‐ATPase
The molecular biological approach has provided important information toward understanding the complexities of the F0F1 ATPase… Expand
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
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
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
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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