Structural insights into an oxalate-producing serine hydrolase with an unusual oxyanion hole and additional lyase activity*

HIGHLIGHTS

• who: Juntaek Oh from the (UNIVERSITY) have published the paper: Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity*, in the Journal: (JOURNAL) of July/15,/2016
• what: The authors report the crystal_structure of Obc1 in its apo and glycerol-bound form at 2.5 Å and 2.8 Å resolution, respectively. This study provides insight into an unusual enzymatic feature, the dual catalytic role of the Obc1 C-domain.
• how: Based on the structural and biochemical data the following reaction mechanism for Obc1 is proposed (Fig . . .
  

   

  

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