Substrate ambiguity among the nudix hydrolases: Biologically significant, evolutionary remnant, or both?

Cellular and Molecular Life Sciences

Volumn 70, Issue 3, 2013, Pages 373-385

  McLennan, Alexander G ^a  

^a UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

Antimutator; Decapping; Diadenosine; Inositol; Nucleotide; Nudix

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; DIADENOSINE HEXAPHOSPHATE; DIADENOSINE PENTAPHOSPHATE; DIADENOSINE TETRAPHOSPHATE; DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE; MESSENGER RNA; MITOCHONDRIAL ENZYME; NUDIX HYDROLASE; PHOSPHATASE; UNCLASSIFIED DRUG;

ADAPTATION; APOPTOSIS; ARABIDOPSIS; ARTICLE; BACILLUS SUBTILIS; BACTERIAL STRAIN; CATALYSIS; DROSOPHILA MELANOGASTER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE DUPLICATION; HUMAN; HYDROLYSIS; MOLECULAR EVOLUTION; MUTAGENICITY; NONHUMAN; PHENOTYPE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RNA DEGRADATION; RNA METABOLISM; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

ACID ANHYDRIDE HYDROLASES; BACTERIA; DEOXYGUANINE NUCLEOTIDES; DINUCLEOSIDE PHOSPHATES; EVOLUTION, MOLECULAR; FUNGI; HUMANS; MUTATION; OXIDATION-REDUCTION; PYROPHOSPHATASES; RNA, MESSENGER; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 84872325981     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1210-3     Document Type: Article

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