Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
Dehydroquinate synthase (DHQS) has long been regarded as a catalytic marvel because of its ability to perform several consecutive chemical reactions in one active site. There has been considerable debate as to whether DHQS is actively involved in all these steps, or whether several steps occur spont...
Κύριοι συγγραφείς: | Carpenter, E, Hawkins, A, Frost, J, Brown, K |
---|---|
Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
1998
|
Παρόμοια τεκμήρια
-
Multistep catalysis dehydroquinate synthase.
ανά: Brown, K, κ.ά.
Έκδοση: (2000) -
Identification of many crystal forms of Aspergillus nidulans dehydroquinate synthase.
ανά: Nichols, C, κ.ά.
Έκδοση: (2001) -
Biophysical and kinetic analysis of wild-type and site-directed mutants of the isolated and native dehydroquinate synthase domain of the AROM protein.
ανά: Park, A, κ.ά.
Έκδοση: (2004) -
Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase.
ανά: Nichols, C, κ.ά.
Έκδοση: (2003) -
Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
ανά: Nichols, C, κ.ά.
Έκδοση: (2004)