Evidence for a Zn2+-binding site in human serum butyrylcholinesterase

Bhanumathy, Cunnigaiper D.; Balasubramanian, A.S.

doi:10.1042/bj3150127

Cited by 17 publications

(3 citation statements)

References 42 publications

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“…Although the mechanism by which ChEs are inhibited by heavy metals is unclear, our results sustain the hypothesis that metal cations inactivate AChE and BChE (Masson et al 1996, Guilhermino et al 1998. Cd 2+ is known to inhibit BChE from human serum (Sarkarati et al 1999) and sheep brain (Çoku-ras & Tezcan 1993) and it has been suggested that human serum BChE has more than one binding motif for divalent cations (Bhanumathy & Balasubramanian 1996.…”

Section: Aquatic Pollutantssupporting

confidence: 86%

Cholinesterase activities in the adductor muscle of the Antarctic scallop Adamussium colbecki

2006

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Antarctica is regarded as one of the most pristine parts of the Earth but even this remote ecosystem is affected by contamination and high levels of certain heavy metals, such as cadmium, which may occur naturally in Antarctic waters. The bivalve scallop Adamussium colbecki is considered a key species of Antarctic benthic ecosystems and a sensitive target for bioaccumulation of xenobiotics and metals. Since cholinesterases (ChEs) in the adductor muscle of A. colbecki presumably play a prominent physiological role through regulation of swimming movements, the main aims of this study was to characterize ChE activities in adductor muscle of A. colbecki and to investigate their sensitivity to organophosphate pesticides and heavy metals. The results suggest that an acetylcholinesterase-like enzyme in the adductor muscle of the scallop has low sensitivity to organophosphates but was significantly inhibited by exposure to cadmium.

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Section: Aquatic Pollutantssupporting

confidence: 86%

Cholinesterase activities in the adductor muscle of the Antarctic scallop Adamussium colbecki

2006

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“…Comparison of the effects of monovalent and divalent ions on the activity of AChE suggests a general screening effect of monovalent cations, while it has been proposed that divalent cations interact specifically with carboxylate groups present in the active site (Hofer et al, 1984). The identification of a putative binding site for Zn 2+ in hBChE (Bhanumathy and Balasubramanian, 1996) supports the notion of specific binding sites for divalent cations in ChEs.…”

Section: Module Ii: the Potential Gradient Along The Active-site Gorgsupporting

confidence: 57%

X-Ray Crystallographic Studies on Acetylcholinesterase and Related Enzymes

Sussman¹,

Silman²

2003

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REPORT DOCUMENTATION PAGEForm ifl burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining ed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for lul&Vn to Washington Headquarters Services, Directorate for Information Operations and Reports, 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302, and TITLE AND SUBTITLE X-Ray Crystallographic Studies on Acetylcholinesterase and Related Enzymes AUTHOR(S)Joel L. Sussman, Ph.D. I. Silman, Ph.D. FUNDING NUMBERS DAMD17-97-2-7022 PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES)Weizmann Institute of Science Rehovot 76100 Israel E-MAIL: j oel.sussman@weizmann. ac.il Where copyrighted material is quoted, permission has been obtained to use such material. PERFORMING ORGANIZATION REPORT NUMBER SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES)UWhere material from documents designated for limited distribution is quoted, permission has been obtained to use the material.Citations of commercial organizations and trade names in this report do not constitute an official Department of Army endorsement or approval of the products or services of these organizations.N/A In conducting research using animals, the investigator(s) adhered to the "Guide for the Care and Use of Laboratory Animals," prepared by the Committee on Care and use of Laboratory Animals of the Institute of Laboratory Resources, national Research Council (NIH Publication No. 86-23, Revised 1985). N/A For the protection of human subjects, the investigator(s) adhered to policies of applicable Federal Law 45 CFR 46. N/A In conducting research utilizing recombinant DNA technology, the investigator(s) adhered to current guidelines promulgated by the National Institutes of Health. N/A Zh the conduct of research utilizing recombinant DNA, the investigator(s) adhered to the NIH Guidelines for Research Involving Recombinant DNA Molecules. N/A In the conduct of research involving hazardous organisms, the investigator(s) adhered to the CDC-NIH Guide for Biosafety in Microbiological and Biomedieal Laboratories.l->r*iA. J J*-»

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“…Comparison of the effects of monovalent and divalent ions on the activity of AChE suggests a general screening effect of monovalent cations, while it has been proposed that divalent cations interact specifically with carboxylate groups present in the active site (Hofer et al, 1984). The identification of a putative binding site for Zn 2ϩ in hBChE (Bhanumathy and Balasubramanian, 1996) supports the notion of specific binding sites for divalent cations in ChEs.…”

Section: Module Ii: the Potential Gradient Along The Active-site Gorge Is Responsible For Steering Cationic Species To The Active Site Ofmentioning

confidence: 71%

A Modular Treatment of Molecular Traffic Through the Active Site of Cholinesterase

Botti¹,

Felder²,

Lifson

et al. 1999

Biophysical Journal

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We present a model for the molecular traffic of ligands, substrates, and products through the active site of cholinesterases (ChEs). First, we describe a common treatment of the diffusion to a buried active site of cationic and neutral species. We then explain the specificity of ChEs for cationic ligands and substrates by introducing two additional components to this common treatment. The first module is a surface trap for cationic species at the entrance to the active-site gorge that operates through local, short-range electrostatic interactions and is independent of ionic strength. The second module is an ionic-strength-dependent steering mechanism generated by long-range electrostatic interactions arising from the overall distribution of charges in ChEs. Our calculations show that diffusion of charged ligands relative to neutral isosteric analogs is enhanced approximately 10-fold by the surface trap, while electrostatic steering contributes only a 1.5- to 2-fold rate enhancement at physiological salt concentration. We model clearance of cationic products from the active-site gorge as analogous to the escape of a particle from a one-dimensional well in the presence of a linear electrostatic potential. We evaluate the potential inside the gorge and provide evidence that while contributing to the steering of cationic species toward the active site, it does not appreciably retard their clearance. This optimal fine-tuning of global and local electrostatic interactions endows ChEs with maximum catalytic efficiency and specificity for a positively charged substrate, while at the same time not hindering clearance of the positively charged products.

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Evidence for a Zn2+-binding site in human serum butyrylcholinesterase

Cited by 17 publications

References 42 publications

Cholinesterase activities in the adductor muscle of the Antarctic scallop Adamussium colbecki

Cholinesterase activities in the adductor muscle of the Antarctic scallop Adamussium colbecki

X-Ray Crystallographic Studies on Acetylcholinesterase and Related Enzymes

A Modular Treatment of Molecular Traffic Through the Active Site of Cholinesterase

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