2. Academic Validation
  3. Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1)

Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1)

  • J Biol Chem. 2001 May 18;276(20):17474-8. doi: 10.1074/jbc.M011569200.
J D Shi 1,  T Kukar,  C Y Wang,  Q Z Li,  P E Cruz,  A Davoodi-Semiromi,  P Yang,  Y Gu,  W Lian,  D H Wu,  J X She
Affiliations

Affiliation

  • 1 Department of Pathology, Immunology and Laboratory Medicine, Center for Mammalian Genetics and Diabetes Center of Excellence, College of Medicine, University of Florida, Gainesville, Florida 32610, USA.
PMID: 11278936 DOI: 10.1074/jbc.M011569200
Abstract

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 approximately 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.

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