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PYP‐1, inorganic pyrophosphatase, is required for larval development and intestinal function in C. elegans
Author(s) -
Ko Kyung Min,
Lee Wonhae,
Yu Jae-Ran,
Ahnn Joohong
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.047
Subject(s) - inorganic pyrophosphatase , caenorhabditis elegans , mutant , pyrophosphatase , pyrophosphate , biology , biochemistry , function (biology) , gene , phenotype , amino acid , enzyme , farnesyl pyrophosphate , larva , phosphate , microbiology and biotechnology , biosynthesis , botany
Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into phosphate (Pi), which provides a thermodynamic driving force for important biosynthetic reactions. The nematode Caenorhabditis elegans gene C47E12.4 encodes a PPase (PYP‐1) which shows 54% amino acid identity with human PPase. PYP‐1 exhibits specific enzyme activity and is mainly expressed in the intestinal and nervous system. A null mutant of pyp‐1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function. The larval arrest phenotype was successfully rescued by reintroduction of the pyp‐1 gene, suggesting that PYP‐1 is required for larval development and intestinal function in C. elegans .