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      Isolation, Identification and Characterization of a Antidementia Acetylcholinesterase Inhibitor-Producing Yarrowia lipolytica S-3

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          Abstract

          This report describes the isolation and identification of a potent acetylcholinesterase (AChE) inhibitor-producing yeasts. Of 731 species of yeast strain, the S-3 strain was selected as a potent producer of AChE inhibitor. The selected S-3 strain was investigated for its microbiological characteristics. The S-3 strain was found to be short-oval yeast that did not form an ascospore. The strain formed a pseudomycelium and grew in yeast malt medium containing 50% glucose and 10% ethanol. Finally, the S-3 strain was identified by its physiological characteristics and 26S ribosomal DNA sequences as Yarrowia lipolytica S-3.

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          Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.

          Victor J. Sussman, L Toker, I Silman … (1991)
          The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.
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            Neuromodulation and cortical function: modeling the physiological basis of behavior.

            Michael E. Hasselmo (1995)
            Neuromodulators including acetylcholine, norepinephrine, serotonin, dopamine and a range of peptides alter the processing characteristics of cortical networks through effects on excitatory and inhibitory synaptic transmission, on the adaptation of cortical pyramidal cells, on membrane potential, on the rate of synaptic modification, and on other cortical parameters. Computational models of self-organization and associative memory function in cortical structures such as the hippocampus, piriform cortex and neocortex provide a theoretical framework in which the role of these neuromodulatory effects can be analyzed. Neuromodulators such as acetylcholine and norepinephrine appear to enhance the influence of synapses from afferent fibers arising outside the cortex relative to the synapses of intrinsic and association fibers arising from other cortical pyramidal cells. This provides a continuum between a predominant influence of external stimulation to a predominant influence of internal recall (extrinsic vs. intrinsic). Modulatory influence along this continuum may underlie effects described in terms of learning and memory, signal to noise ratio, and attention.
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              A molecular link between the active component of marijuana and Alzheimer's disease pathology.

              Lisa M Eubanks, Claude J Rogers, Albert E Beuscher … (2006)
              Alzheimer's disease is the leading cause of dementia among the elderly, and with the ever-increasing size of this population, cases of Alzheimer's disease are expected to triple over the next 50 years. Consequently, the development of treatments that slow or halt the disease progression have become imperative to both improve the quality of life for patients and reduce the health care costs attributable to Alzheimer's disease. Here, we demonstrate that the active component of marijuana, Delta9-tetrahydrocannabinol (THC), competitively inhibits the enzyme acetylcholinesterase (AChE) as well as prevents AChE-induced amyloid beta-peptide (Abeta) aggregation, the key pathological marker of Alzheimer's disease. Computational modeling of the THC-AChE interaction revealed that THC binds in the peripheral anionic site of AChE, the critical region involved in amyloidgenesis. Compared to currently approved drugs prescribed for the treatment of Alzheimer's disease, THC is a considerably superior inhibitor of Abeta aggregation, and this study provides a previously unrecognized molecular mechanism through which cannabinoid molecules may directly impact the progression of this debilitating disease.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Mycobiology
                Journal ID (iso-abbrev): Mycobiology
                Journal ID (publisher-id): MB
                Title: Mycobiology
                Publisher: The Korean Society of Mycology
                ISSN (Print): 1229-8093
                ISSN (Electronic): 2092-9323
                Publication date (Print): March 2012
                Publication date (Electronic): 31 March 2012
                Volume: 40
                Issue: 1
                Pages: 42-46
                Affiliations
                [1 ]Department of Life Science and Genetic Engineering, PaiChai University, Daejeon 302-735, Korea.
                [2 ]Department of Bio-Environmental Chemistry, Chungnam National University, Daejeon 305-764, Korea.
                [3 ]Microbial and Enzymatic Technology Group, Bioprocess Platform, Biotechnology Research Institite, National Research Council of Canada, Montreal, QC H4P2R2, Canada.
                Author notes
                Corresponding author ( biotech8@ 123456pcu.ac.kr )
                Article
                DOI: 10.5941/MYCO.2012.40.1.042
                PMC ID: 3385141
                PubMed ID: 22783133
                SO-VID: 889f980b-2abe-40ae-8034-76e80112ee35
                Copyright © © The Korean Society of Mycology
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 16 February 2012
                Date revision received : 05 March 2012
                Date accepted : 09 March 2012
                Categories
                Subject: Research Article

                ScienceOpen disciplines: Plant science & Botany
                Keywords: yarrowia lipolytica s-3,26s rdna sequences,antidementia acetylcholinesterase inhibitor
                Data availability:
                ScienceOpen disciplines: Plant science & Botany
                Keywords: yarrowia lipolytica s-3, 26s rdna sequences, antidementia acetylcholinesterase inhibitor

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