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'''Lactacystin''' is an ] naturally ] by ] of the ] '']'' first identified as an inducer of neuritogenesis in neuroblastoma cells in 1991.<ref name="Omura">Omura S, Fujimoto T, Otoguro K, Matsuzaki K, Moriguchi R, Tanaka H, Sasaki Y. (1991). Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells: S. Omura, et al. ''J. Antibiot.'' 44(1):113-6.</ref> The target of lactacystin was subsequently found to be the ] on the basis of its affinity for certain catalytic subunits of the proteasome by Fenteany and co-workers in 1995.<ref name="Fenteany1">{{cite journal |vauthors=Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL |title=Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin |journal=Science |volume=268 |issue=5211 |pages=726–31 |year=1995 |pmid=7732382 |doi=10.1126/science.7732382|bibcode=1995Sci...268..726F |s2cid=37779687 }}</ref> The proteasome is a protein complex responsible for the bulk of proteolysis in the cell, as well as proteolytic activation of certain protein substrates. Lactacystin was the first non-peptidic proteasome inhibitor discovered and is widely used as a research tool in biochemistry and cell biology. The transformation product of lactacystin clasto-lactacystin β-lactone (also known as omuralide) covalently modifies the amino-terminal threonine of specific catalytic subunits of the proteasome, a discovery that helped to establish the proteasome as a mechanistically novel class of protease: an amino-terminal ]. The molecule is commonly used in ] and ] laboratories as a selective inhibitor of the ].<ref name="Fenteany1">{{cite journal |vauthors=Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL |title=Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin |journal=Science |volume=268 |issue=5211 |pages=726–31 |year=1995 |pmid=7732382 |doi=10.1126/science.7732382|bibcode=1995Sci...268..726F |s2cid=37779687 }}</ref><ref name="Fenteany2">{{cite journal |vauthors=Fenteany G, Schreiber SL |title=Lactacystin, proteasome function, and cell fate |journal=J. Biol. Chem. |volume=273 |issue=15 |pages=8545–8 |year=1998 |pmid= 9535824 |doi=10.1074/jbc.273.15.8545|doi-access= }}</ref> The first ] of lactacystin was developed in 1992 by Corey and Reichard,<ref name="Corey">''"Total Synthesis of Lactacystin"'' Corey, E. J.; Reichard, G. A. '']'' '''1992''', ''114'', 10677.</ref> and a number of other syntheses of this molecule have also been published. There are more than 1,660 entries for lactacystin in ] as of January 2019. |
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'''Lactacystin''' is an ] naturally ] by ] of the ] '']'' first identified as an inducer of neuritogenesis in neuroblastoma cells in 1991.<ref name="Omura">Omura S, Fujimoto T, Otoguro K, Matsuzaki K, Moriguchi R, Tanaka H, Sasaki Y. (1991). Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells: S. Omura, et al. ''J. Antibiot.'' 44(1):113-6.</ref> The target of lactacystin was subsequently found to be the ] on the basis of its affinity for certain catalytic subunits of the proteasome by Fenteany and co-workers in 1995.<ref name="Fenteany1">{{cite journal |vauthors=Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL |title=Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin |journal=Science |volume=268 |issue=5211 |pages=726–31 |year=1995 |pmid=7732382 |doi=10.1126/science.7732382|bibcode=1995Sci...268..726F |s2cid=37779687 }}</ref> The proteasome is a protein complex responsible for the bulk of proteolysis in the cell, as well as proteolytic activation of certain protein substrates. Lactacystin was the first non-peptidic proteasome inhibitor discovered and is widely used as a research tool in biochemistry and cell biology. The transformation product of lactacystin clasto-lactacystin β-lactone (also known as omuralide) covalently modifies the amino-terminal threonine of specific catalytic subunits of the proteasome, a discovery that helped to establish the proteasome as a mechanistically novel class of protease: an amino-terminal ]. The molecule is commonly used in ] and ] laboratories as a selective inhibitor of the ].<ref name="Fenteany1">{{cite journal |vauthors=Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL |title=Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin |journal=Science |volume=268 |issue=5211 |pages=726–31 |year=1995 |pmid=7732382 |doi=10.1126/science.7732382|bibcode=1995Sci...268..726F |s2cid=37779687 }}</ref><ref name="Fenteany2">{{cite journal |vauthors=Fenteany G, Schreiber SL |title=Lactacystin, proteasome function, and cell fate |journal=J. Biol. Chem. |volume=273 |issue=15 |pages=8545–8 |year=1998 |pmid= 9535824 |doi=10.1074/jbc.273.15.8545|doi-access= free}}</ref> The first ] of lactacystin was developed in 1992 by Corey and Reichard,<ref name="Corey">''"Total Synthesis of Lactacystin"'' Corey, E. J.; Reichard, G. A. '']'' '''1992''', ''114'', 10677.</ref> and a number of other syntheses of this molecule have also been published. There are more than 1,660 entries for lactacystin in ] as of January 2019. |
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