Sanbox Reserved 684: Difference between revisions
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The side chain amino group of Orn attacks the carbonyl carbon of CP nucleophillically, to form a tetrahedral transition state. A charge rearrangement then realeases Cit and Pi. | The side chain amino group of Orn attacks the carbonyl carbon of CP nucleophillically, to form a tetrahedral transition state. A charge rearrangement then realeases Cit and Pi. | ||
N5-Phosphonoacetyl-l-ornithine (PALO, 1) is a bisubstrate transition-state analog which competitively inhibits ornithine transcarbamylase (OTC) in vitro.<ref>http://www.google.com/url?sa=t&rct=j&q=&esrc=s&source=web&cd=1&ved=0CDMQFjAA&url=http%3A%2F%2Fdigitalcommons.unl.edu%2Fcgi%2Fviewcontent.cgi%3Farticle%3D1009%26context%3Dchemistrydussault&ei=00qkUPOCIYqs9ATd9YHwBQ&usg=AFQjCNH-HXNQ5-7yov_T0Z-TGxDhjGAXyQ</ref>Studies have also shown that N δ-(N′-sulfodiaminophosphinyl)-l-ornithine (PSOrn), with its three unique N-P bonds, represents a true transition state analogue for ornithine transcarbamoylases (OTC)<ref>http://www.jbc.org/content/275/26/20012</ref>. Another inhibitor being studied is The inhibition of ornithine transcarbamoylase from Escherichia coli W by phaseolotoxin. In the presence of phaseolotoxin ornithine transcarbamoylase exhibited a transient phase of activity before a steady state. | N5-Phosphonoacetyl-l-ornithine (PALO, 1) is a bisubstrate transition-state analog which competitively inhibits ornithine transcarbamylase (OTC) in vitro.<ref>http://www.google.com/url?sa=t&rct=j&q=&esrc=s&source=web&cd=1&ved=0CDMQFjAA&url=http%3A%2F%2Fdigitalcommons.unl.edu%2Fcgi%2Fviewcontent.cgi%3Farticle%3D1009%26context%3Dchemistrydussault&ei=00qkUPOCIYqs9ATd9YHwBQ&usg=AFQjCNH-HXNQ5-7yov_T0Z-TGxDhjGAXyQ</ref>Studies have also shown that N δ-(N′-sulfodiaminophosphinyl)-l-ornithine (PSOrn), with its three unique N-P bonds, represents a true transition state analogue for ornithine transcarbamoylases (OTC)<ref>http://www.jbc.org/content/275/26/20012</ref>. Another inhibitor being studied is The inhibition of ornithine transcarbamoylase from Escherichia coli W by phaseolotoxin. In the presence of phaseolotoxin ornithine transcarbamoylase exhibited a transient phase of activity before a steady state.<ref>http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1144443/)</ref> | ||
References: {{reflist}} | References: {{reflist}} | ||