Download citation
Download citation
link to html
A snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of kcat and KM are 31.1 s-1 and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 Å) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I213, with unit-cell parameter a = 169.31 Å, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 Å3 Da-1. The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom.

Supporting information

PDB reference: AHP-LAAO, 1reo, r1reosf


Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds