title: Characterization of a cadmium-inducible isoform of pyruvate carboxylase from Caenorhabditis elegans.
abstract: A homologue of pyruvate carboxylase was isolated as an expressed sequence tag during the identification of cadmium-responsive genes in Caenorhabditis elegans. The C. elegans protein, designated PYC-1, is predicted to contain 1,175 amino acids with a molecular mass of 129,284. Amino acid sequence analysis indicates that PYC-1 will be translocated into mitochondria. PYC-1 has high levels of amino acid sequence identity with other pyruvate carboxylases. The highest levels of identity are in the putative transcarboxylation, biotin carboxylation and biotin carboxyl carrier domains.
authors.affiliation: Nicholas School of the Environment, Box 90328, Duke University, Durham, North Carolina 27708-0328, USA.
authors.forename: V H
authors.initials: VH
authors.lastname: Liao
authors.forename: J H
authors.initials: JH
authors.lastname: Freedman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002104:Cadmium / Q000494:pharmacology*; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects*; D007527:Isoenzymes; D008969:Molecular Sequence Data; D011766:Pyruvate Carboxylase / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D007527:Isoenzymes; D002104:Cadmium; D011766:Pyruvate Carboxylase