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Exploring Allosteric Activation Of Ligab From Sphingobium Sp. Strain Syk-6 Through Kinetics, Mutagenesis And Computational Studies, Kevin P. Barry, Jason P. Gerbino, Abraham Ngu, Erin F. Cohn, Joy M. Cote, A. Maxwell Burroughs, Erika A. Taylor
Exploring Allosteric Activation Of Ligab From Sphingobium Sp. Strain Syk-6 Through Kinetics, Mutagenesis And Computational Studies, Kevin P. Barry, Jason P. Gerbino, Abraham Ngu, Erin F. Cohn, Joy M. Cote, A. Maxwell Burroughs, Erika A. Taylor
Erika A. Taylor, Ph.D.
The protocatechuate 4,5-dioxygenase (LigAB) from Sphingobium sp. strain SYK-6 is the defining member of the Type II extradiol dioxygenase superfamily (a.k.a. PCA Dioxygenase Superfamily or PCADSF) and plays a key aromatic ring-opening role in the metabolism of several lignin derived aromatic compounds. In our search for alternate substrates and inhibitors of LigAB, we discovered allosteric rate enhancement in the presence of non-substrate protocatechuate-like aldehydes such as vanillin. LigAB has the broadest substrate utilization profile of all protocatechuate (PCA) 4,5-dioxygenase described in the literature, however, the rate enhancement is only observed with PCA, with vanillin increasing kcat for LigAB by 36%. …