The mechanism of glutamine-dependent amidotransferases |
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Authors: | F Massière M-A Badet-Denisot |
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Institution: | (1) Institut de Chimie des Substances Naturelles, C.N.R.S. UPR 2301, F-91198 Gif-sur-Yvette Cedex (France), Fax +33 169 07 72 72 47, e-mail: Marie-Ange.Badet@icsn.cnrs-gif.fr, FR |
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Abstract: | Glutamine-dependent amidotransferases have been known for more than 30 years. The mechanism by which these enzymes generate
ammonia from the glutamine amide nitrogen and transfer it to seven different chemical classes of acceptors has been the subject
of intense scrutiny for the last 5 years. The increasing number of biochemical and structural studies dealing with amidotransferases
and with mechanistically related enzymes has disclosed the dichotomy of the mechanisms within these enzymes for achieving
the glutamine amide bond cleavage. Some of them use a catalytic Cys/His/Glu triad similar to serine protease, whereas the
aminoterminal cysteine of the others is believed to play the same function. The transfer of ammonia from the glutamine site
to the acceptor site which must operate in a concerted manner has been demonstrated in two cases to involve channelling but
is still matter of investigation. |
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Keywords: | , Glutamine-dependent amidotransferase, catalytic mechanism, ammonia transfer, |
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