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Chloride promotes refolding of active Vibrio alkaline phosphatase through an inactive dimeric intermediate with an altered interface

Hjörleifsson, Jens G; Ásgeirsson, Bjarni (Wiley, 2018-12-21)

Most enzymes are homodimers or higher order multimers. Cold‐active alkaline phosphatase from Vibrio splendidus (VAP) transitions into a dimer with very low activity under mild denaturation conditions. The desire to understand why this dimer fails to ...
Cold-active alkaline phosphatase is irreversibly transformed into an inactive dimer by low urea concentrations

Hjörleifsson, Jens G; Ásgeirsson, Bjarni (Elsevier BV, 2016-07)

Alkaline phosphatase is a homodimeric metallo-hydrolase where both Zn2+ and Mg2+ are important for catalysis and stability. Cold-adapted alkaline phosphatase variants have high activity at low temperatures and lower thermal stability compared with ...
pH-Dependent Binding of Chloride to a Marine Alkaline Phosphatase Affects the Catalysis, Active Site Stability, and Dimer Equilibrium

Hjörleifsson, Jens G; Ásgeirsson, Bjarni (American Chemical Society (ACS), 2017-09-07)

The effect of ionic strength on enzyme activity and stability varies considerably between enzymes. Ionic strength is known to affect the catalytic activity of some alkaline phosphatases (APs), such as Escherichia coli AP, but how ions affect APs is ...

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