PAD2 Activity Monitored via a Fluorescent Substrate Analog

2015 ◽  
Vol 86 (4) ◽  
pp. 599-605
Author(s):  
Mary J. Sabulski ◽  
Yanming Wang ◽  
Marcos M. Pires
Keyword(s):  
Fluorescent Substrate ◽  
Substrate Analog

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

2011 ◽  
Vol 417 (1) ◽  
pp. 136-141 ◽  
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

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

1996 ◽  
Vol 40 (7) ◽  
pp. 1640-1644 ◽  
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.

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

Biochemistry ◽  
1981 ◽  
Vol 20 (11) ◽  
pp. 3103-3109 ◽  
Author(s):  
Gedalyahu Skorka ◽  
Pessia Shuker ◽  
David Gill ◽  
Jacob Zabicky ◽  
Abraham H. Parola
Keyword(s):  
Adenosine Deaminase ◽  
Fluorescent Substrate ◽  
Substrate Analog

β-Amyrin biosynthesis: catalytic mechanism and substrate recognition

2017 ◽  
Vol 15 (14) ◽  
pp. 2869-2891 ◽  
Author(s):  
Tsutomu Hoshino
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
The Past ◽  
Substrate Analog ◽  
Analog Experiments

In the past five years, there have been remarkable advances in the study of β-amyrin synthase. This review outlines the catalytic mechanism and substrate recognition in β-amyrin biosynthesis, which have been attained by the site-directed mutagenesis and substrate analog experiments.

Virtual Screening and X-ray Crystallography Identify Non-Substrate Analog Inhibitors of Flavin-Dependent Thymidylate Synthase

2016 ◽  
Vol 59 (19) ◽  
pp. 9269-9275 ◽  
Author(s):  
Rosaria Luciani ◽  
Puneet Saxena ◽  
Sachin Surade ◽  
Matteo Santucci ◽  
Alberto Venturelli ◽  
...  
Keyword(s):  
Virtual Screening ◽  
Thymidylate Synthase ◽  
X Ray ◽  
X Ray Crystallography ◽  
Substrate Analog
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