Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Gedalyahu Skorka; Pessia Shuker; David Gill; Jacob Zabicky; Abraham H. Parola

doi:10.1021/bi00514a018

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Biochemistry ◽

10.1021/bi00514a018 ◽

1981 ◽

Vol 20 (11) ◽

pp. 3103-3109 ◽

Cited By ~ 24

Author(s):

Gedalyahu Skorka ◽

Pessia Shuker ◽

David Gill ◽

Jacob Zabicky ◽

Abraham H. Parola

Keyword(s):

Adenosine Deaminase ◽

Fluorescent Substrate ◽

Substrate Analog

Download Full-text

Binding of the fluorescent substrate analog 2',3'-O-(2,4,6-trinitrophenylcyclohexadienylidene)adenosine 5'-triphosphate to the gastric hydrogen ion-potassium-ATPase: evidence for cofactor-induced conformational changes in the enzyme

Biochemistry ◽

10.1021/bi00465a004 ◽

1990 ◽

Vol 29 (13) ◽

pp. 3179-3186 ◽

Cited By ~ 23

Author(s):

Larry D. Faller

Keyword(s):

Conformational Changes ◽

Hydrogen Ion ◽

Fluorescent Substrate ◽

Substrate Analog ◽

Potassium Atpase

Download Full-text

Fluorescent substrate analog for monitoring chain elongation by undecaprenyl pyrophosphate synthase in real time

Analytical Biochemistry ◽

10.1016/j.ab.2011.05.043 ◽

2011 ◽

Vol 417 (1) ◽

pp. 136-141 ◽

Cited By ~ 6

Author(s):

Kuo-Hsun Teng ◽

Annie P.-C. Chen ◽

Chih-Jung Kuo ◽

Yu-Chin Li ◽

Hon-Ge Liu ◽

...

Keyword(s):

Real Time ◽

Chain Elongation ◽

Fluorescent Substrate ◽

Substrate Analog

Download Full-text

Adenosine deaminase in the marine mussel, Mytilus edulis: Purification, characterization and inhibition by a substrate analog, coformycin

Comparative Biochemistry and Physiology Part B Comparative Biochemistry ◽

10.1016/0305-0491(84)90239-6 ◽

1984 ◽

Vol 77 (1) ◽

pp. 167-173 ◽

Cited By ~ 4

Author(s):

Yoko Aikawa ◽

Toyoo Aikawa

Keyword(s):

Adenosine Deaminase ◽

Mytilus Edulis ◽

Marine Mussel ◽

Substrate Analog

Download Full-text

N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 2. Fast-reaction studies show that a fluorescent substrate analog binds independently to two different sites

Biochemistry ◽

10.1021/bi00593a030 ◽

1979 ◽

Vol 18 (26) ◽

pp. 5953-5959 ◽

Cited By ~ 18

Author(s):

Willy Cohn ◽

Kasper Kirschner ◽

Carlton Paul

Keyword(s):

Fast Reaction ◽

Fluorescent Substrate ◽

Substrate Analog ◽

Phosphate Synthase

Download Full-text

Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli.

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.40.7.1640 ◽

1996 ◽

Vol 40 (7) ◽

pp. 1640-1644 ◽

Cited By ~ 137

Author(s):

P E Brandish ◽

K I Kimura ◽

M Inukai ◽

R Southgate ◽

J T Lonsdale ◽

...

Keyword(s):

Escherichia Coli ◽

Antibacterial Agents ◽

Enzyme Assay ◽

Molecular Mechanisms ◽

Fluorescent Substrate ◽

Acceptor Substrate ◽

Nucleoside Antibiotics ◽

Substrate Analog ◽

Binding Inhibition ◽

Insight Into

Using a continuous fluorescence-based enzyme assay, we have characterized the antibacterial agents tumicamycin and liposidomycin B as inhibitors of solubilized Escherichia coli phospho-N-acetylmuramyl-pentapeptide translocase. Tunicamycin exhibited reversible inhibition (Ki = 0.55 +/- 0.1 microM) which was noncompetitive with respect to the lipid acceptor substrate and competitive with respect to the fluorescent substrate analog, dansyl-UDPMurNAc-pentapeptide. Liposidomycin B exhibited slow-binding inhibition (Ki = 80 +/- 15 nM) which was competitive with respect to the lipid acceptor substrate and noncompetitive with respect to dansyl-UDPMurNAc-pentapeptide. These results provide insight into the molecular mechanisms of action of these two classes of nucleoside antibiotics.

Download Full-text