| First Author | Shi JD | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 20 | Pages | 17474-8 |
| PubMed ID | 11278936 | Mgi Jnum | J:69495 |
| Mgi Id | MGI:1934730 | Doi | 10.1074/jbc.M011569200 |
| Citation | Shi JD, et al. (2001) Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1). J Biol Chem 276(20):17474-8 |
| abstractText | 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. |
