scholarly journals Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding

2015 ◽  
Vol 6 (7) ◽  
pp. 4060-4065 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Jonas Schätti ◽  
Edward Stuttfeld ◽  
Kei Ohkubo ◽  
Timm Maier ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
Metal Cofactor

Adding a metal cofactor to a protein bearing a latent metal binding site endows the macromolecule with nascent catalytic activity.

scholarly journals A conserved regulatory switch controls phosphatase activity and specificity

2019 ◽  
Author(s):  
Kristin Ho ◽  
Niels Bradshaw
Keyword(s):  
Bacillus Subtilis ◽  
Substrate Specificity ◽  
Binding Site ◽  
Phosphatase Activity ◽  
Metal Binding ◽  
Regulatory Mechanism ◽  
Metal Binding Site ◽  
Essential Metal ◽  
Cofactor Binding ◽  
Metal Cofactor

AbstractProtein phosphatases must be regulated and specific for their substrates; how this control is achieved is critical for signaling by reversible phosphorylation. We recently reported the discovery of a regulatory switch that controls the activity of the PP2C family serine/threonine phosphatase SpoIIE from the bacterium Bacillus subtilis. This regulatory switch activates SpoIIE during spore development by forming the catalytically essential metal-binding site that is conserved across the PP2C family. We hypothesized that this switch is a conserved platform for regulating other PP2C phosphatases. An orthologous phosphatase from B. subtilis, RsbU, is activated under stress conditions and responds to different signals and acts on a different phosphoprotein substrate than SpoIIE. Using a combination of biochemical and genetic approaches, we find that broad features of the regulatory mechanism are conserved between SpoIIE and RsbU but that each phosphatase has adapted its response to be most appropriate for the distinct biological outputs it controls. In both cases, the switch accomplishes this by integrating substrate binding and recognition with regulatory inputs to control metal cofactor binding and catalysis. Thus, the switch is a conserved and mechanistically flexible regulatory platform that controls phosphatase activity and substrate specificity.

Unraveling the Substrate−Metal Binding Site of Ferrochelatase:  An X-ray Absorption Spectroscopic Study†

Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 4809-4818 ◽  
Author(s):  
Gloria C. Ferreira ◽  
Ricardo Franco ◽  
Arianna Mangravita ◽  
Graham N. George
Keyword(s):  
Spectroscopic Study ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
X Ray ◽  
Substrate Metal ◽  
X Ray Absorption

Construction of an additional metal-binding site in human metallothionein-2

2006 ◽  
Vol 101 (4) ◽  
pp. 354-360 ◽  
Author(s):  
Mitsutoshi Toyama ◽  
Mariko Sasaki ◽  
Noriaki Hirayama ◽  
Yoshikatsu Murooka ◽  
Mitsuo Yamashita
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site
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