• The high catalytic rate of the cold-active Vibrio alkaline phosphatase requires a hydrogen bonding network involving a large interface loop 

      Hjörleifsson, Jens Guðmundur; Helland, Ronny; Magnusdottir, Manuela; Ásgeirsson, Bjarni (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-11-16)
      The role of surface loops in mediating communication through residue networks is still a relatively poorly understood part in the study of cold adaptation of enzymes, especially in terms of their quaternary interactions. Alkaline phosphatase (AP) from the psychrophilic marine bacterium <i>Vibrio splendidus</i> (VAP) is characterized by an analogous large surface loop in each monomer, referred to as ...
    • X-ray crystal structure of Vibrio alkaline phosphatase with the non-competitive inhibitor cyclohexylamine 

      Ásgeirsson, Bjarni; Markússon, Sigurbjörn; Hlynsdóttir, Sigríður S.; Helland, Ronny; Hjörleifsson, Jens G. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-10-15)
      <i>Background</i> - <i>Para</i>-nitrophenyl phosphate, the common substrate for alkaline phosphatase (AP), is available as a cyclohexylamine salt. Here, we report that cyclohexylamine is a non-competitive inhibitor of APs.<br><br> <i>Methods</i> - Cyclohexylamine inhibited four different APs. Co-crystallization with the cold-active <i>Vibrio</i> AP (VAP) was performed and the structure solved.<br><br> ...