Molecular Cloning and Characterization of a Novel Mammalian Endo-apyrase (LALP1)

Jing Da Shi, Thomas Kukar, Cong Yi Wang, Quan Zhen Li, Pedro E. Cruz, Abdoreza Davoodi-Semiromi, Ping Yang, Yunrong Gu, Wei Lian, Donghai H. Wu, Jin-Xiong She

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Here we describe the cloning, localization, and characterization of a novel mammalian endo-apyrase (LALP1) in human and mouse. The predicted human LALP1 gene encodes a 604-amino acid protein, whereas the mouse Lalp1 gene encodes a 606-amino acid protein. The human and mouse genes have 88% amino acid sequence identity. These genes share considerable homologies with hLALP70, a recently discovered mammalian lysosomal endo-apyrase. The human LALP1 gene resides on chromosome 10q23-q24 and contains 12 exons and 11 introns covering a genomic region of ∼46 kilobase pairs. The subcellular localization and enzymatic activity of LALP1 indicated that LALP1 is indeed an endo-apyrase with substrate preference for nucleoside triphosphates UTP, GTP, and CTP.

Original languageEnglish (US)
Pages (from-to)17474-17478
Number of pages5
JournalJournal of Biological Chemistry
Issue number20
StatePublished - May 18 2001
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Shi, J. D., Kukar, T., Wang, C. Y., Li, Q. Z., Cruz, P. E., Davoodi-Semiromi, A., Yang, P., Gu, Y., Lian, W., Wu, D. H., & She, J-X. (2001). Molecular Cloning and Characterization of a Novel Mammalian Endo-apyrase (LALP1). Journal of Biological Chemistry, 276(20), 17474-17478.