Literature DB >> 11278936

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

J D Shi1, 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.   

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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Year:  2001        PMID: 11278936     DOI: 10.1074/jbc.M011569200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  17 in total

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5.  N-linked oligosaccharides affect the enzymatic activity of CD39: diverse interactions between seven N-linked glycosylation sites.

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Review 9.  Possible effects of microbial ecto-nucleoside triphosphate diphosphohydrolases on host-pathogen interactions.

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