Kinetic and physical characterization of the inducible UDP-N- acetylglucosamine pyrophosphorylase from Giardia intestinalis

Journal of Biological Chemistry

Volumn 280, Issue 47, 2005, Pages 39363-39372

  Mok, Myth T S ^a   Edwards, Michael R ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSTS; PHOSPHATES; PHYSIOLOGY; PROTEINS; SUBSTRATES; SYNTHESIS (CHEMICAL);

EUKARYOTIC UAPS; GIARDIA INTESTINALIS; GIARDIA INTESTINALIS (GIUAP); MALDI MASS SPECTROMETRY; PYROPHOSPHATE SYNTHESIS; SIZE-EXCLUSION CHROMATOGRAPHY; SYST WALL SYNTHESIS; THERMAL DENATURATION ANALYSIS; UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE; URIDINE-BASED NUCLEOTIDES;

ENZYMES;

ALANINE; GLYCINE; N ACETYLGALACTOSAMINE; PHOSPHORYLASE; PYROPHOSPHATE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; URIDINE DERIVATIVE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE PYROPHOSPHORYLASE; URIDINE TRIPHOSPHATE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME INDUCTION; ENZYME KINETICS; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; GIARDIA LAMBLIA; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STABILITY; WESTERN BLOTTING;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CATALYTIC DOMAIN; DNA, PROTOZOAN; ENZYME INDUCTION; ENZYME STABILITY; GIARDIA LAMBLIA; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEOTIDYLTRANSFERASES; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; URIDINE TRIPHOSPHATE;

EUKARYOTA; GIARDIA; GIARDIA INTESTINALIS;

EID: 28244446959     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M509209200     Document Type: Article

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