A unique dual activity amino acid hydroxylase in Toxoplasma gondii

PLoS ONE

Volumn 4, Issue 3, 2009, Pages

  Gaskell, Elizabeth A ^a   Smith, Judith E ^a   Pinney, John W ^b   Westhead, David R ^a   McConkey, Glenn A ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC LEVO AMINO ACID DECARBOXYLASE; PHENYLALANINE; TYROSINE; TYROSINE 3 MONOOXYGENASE; TYROSINE 3 MONOOXYGENASE 1; TYROSINE 3 MONOOXYGENASE 2; UNCLASSIFIED DRUG; 6 METHYLTETRAHYDROPTERIN; 6-METHYLTETRAHYDROPTERIN; HYBRID PROTEIN; MESSENGER RNA; PHENYLALANINE 4 MONOOXYGENASE; PROTOZOAL PROTEIN; PROTOZOAL RNA; PTERIN DERIVATIVE;

AMINO TERMINAL SEQUENCE; APICOMPLEXAN LIFE CYCLE STAGE; ARTICLE; BRADYZOITE; CONTROLLED STUDY; CRYPTOSPORIDIUM; EIMERIA; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME METABOLISM; ENZYME SUBSTRATE; GENE EXPRESSION; GENE SEQUENCE; GENETIC CONSERVATION; GENOME ANALYSIS; NEOSPORA CANINUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMODIUM; PROTEIN MOTIF; THEILERIA; TOXOPLASMA GONDII; AMINO ACID SEQUENCE; ANIMAL; BIOSYNTHESIS; COMPARATIVE STUDY; ENZYME SPECIFICITY; ENZYMOLOGY; FIBROBLAST; GENE; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; HUMAN; METABOLISM; MOLECULAR GENETICS; PARASITOLOGY; RAT; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; TOXOPLASMA;

CRYPTOSPORIDIUM; EIMERIA; METAZOA; NEOSPORA CANINUM; PROTOZOA; THEILERIA; TOXOPLASMA GONDII;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; FIBROBLASTS; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENES, PROTOZOAN; HUMANS; MOLECULAR SEQUENCE DATA; PHENYLALANINE; PHENYLALANINE HYDROXYLASE; PROTOZOAN PROTEINS; PTERINS; RATS; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; RNA, PROTOZOAN; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY; TOXOPLASMA; TYROSINE; TYROSINE 3-MONOOXYGENASE;

EID: 62849121535     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004801     Document Type: Article

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