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Full-Text Articles in Physical Sciences and Mathematics
Structural Basis For Catalysis By The Mono- And Dimetalated Forms Of The Dape-Encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase, Boguslaw Nocek, Danuta Gillner, Yao Fan, Richard Holz, Andzrej Joachimiak
Structural Basis For Catalysis By The Mono- And Dimetalated Forms Of The Dape-Encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase, Boguslaw Nocek, Danuta Gillner, Yao Fan, Richard Holz, Andzrej Joachimiak
Richard C. Holz
Biosynthesis of lysine and meso-diaminopimelic acid in bacteria provides essential components for protein synthesis and construction of the bacterial peptidoglycan cell wall. The dapE operon enzymes synthesize both meso-diaminopimelic acid and lysine and, therefore, represent potential targets for novel antibacterials. The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase functions in a late step of the pathway and converts N-succinyl-l,l-diaminopimelic acid to l,l-diaminopimelic acid and succinate. Deletion of the dapE gene is lethal to Helicobacter pylori and Mycobacterium smegmatis, indicating that DapE's are essential for cell growth and proliferation. Since there are no similar pathways in humans, inhibitors …
The Fe-Type Nitrile Hydratase From Comamonas Testosteroni Ni1 Does Not Require An Activator Accessory Protein For Expression In Escherichia Coli, Misty Kuhn, Salette Martinez, Natalie Gumataotao, Uwe Bornscheuer, Dali Liu, Richard Holz
The Fe-Type Nitrile Hydratase From Comamonas Testosteroni Ni1 Does Not Require An Activator Accessory Protein For Expression In Escherichia Coli, Misty Kuhn, Salette Martinez, Natalie Gumataotao, Uwe Bornscheuer, Dali Liu, Richard Holz
Richard C. Holz
We report herein the functional expression of an Fe-type nitrile hydratase (NHase) without the co-expression of an activator protein or the Escherichia coli chaperone proteins GroES/EL. Soluble protein was obtained when the α- and β-subunit genes of the Fe-type NHase Comamonas testosteroni Ni1 (CtNHase) were synthesized with optimized E. coli codon usage and co-expressed. As a control, the Fe-type NHase from Rhodococcus equi TG328–2 (ReNHase) was expressed with (ReNHase+Act) and without (ReNHase−Act) its activator protein, establishing that expression of a fully functional, metallated ReNHase enzyme requires the co-expression of its activator protein, similar to all other Fe-type NHase enzymes reported …