Document Detail

Boric acid inhibits adenosine diphosphate-ribosyl cyclase non-competitively.
MedLine Citation:
PMID:  16545389     Owner:  NLM     Status:  MEDLINE    
Adenosine diphosphate-ribosyl cyclase (ADP-ribosyl cyclase) is a ubiquitous enzyme in eukaryotes that converts NAD+ to cyclic-ADP-ribose (cADPR) and nicotinamide. A quantitative assay for cADPR was developed using capillary electrophoresis to separate NAD+, cADPR, ADP-ribose, and ADP with UV detection (254 nm). Using this assay, the apparent Km and Vmax for Aplysia ADP-ribosyl cyclase were determined to be 1.24+/-0.05 mM and 131.8+/-2.0 microM/min, respectively. Boric acid inhibited ADP-ribosyl cyclase non-competitively with a Ki of 40.5+/-0.5 mM. Boric acid binding to cADPR, determined by electrospray ionization mass spectrometry, was characterized by an apparent binding constant, KA, of 655+/-99 L/mol at pH 10.3.
Danny H Kim; Shane Que Hee; Andrew J Norris; Kym F Faull; Curtis D Eckhert
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-03-20
Journal Detail:
Title:  Journal of chromatography. A     Volume:  1115     ISSN:  0021-9673     ISO Abbreviation:  J Chromatogr A     Publication Date:  2006 May 
Date Detail:
Created Date:  2006-05-01     Completed Date:  2006-07-19     Revised Date:  2009-01-15    
Medline Journal Info:
Nlm Unique ID:  9318488     Medline TA:  J Chromatogr A     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  246-52     Citation Subset:  IM    
Department of Environmental Health Sciences, Box 951772, University of California, 650 Charles E Young Dr South, Los Angeles, CA 90095-1772, USA.
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MeSH Terms
ADP-ribosyl Cyclase / antagonists & inhibitors*,  isolation & purification
Aplysia / enzymology
Boric Acids / pharmacology*
Electrophoresis, Capillary
Spectrometry, Mass, Electrospray Ionization
Reg. No./Substance:
0/Boric Acids; 11113-50-1/boric acid; EC Cyclase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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