Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate deaminase of Escherichia coli induced by active or allosteric site ligands at steady state

Biochemistry

Volumn 44, Issue 46, 2005, Pages 15083-15092

  Sosa Peinado, Alejandro ^a   González Andrade, Martín ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ENZYMES; ESCHERICHIA COLI; FLUORESCENCE; INTERFACES (MATERIALS); MATHEMATICAL MODELS; MUTAGENESIS; PHOSPHATES;

ALLOSTERIC SITE; ALLOSTERIC TRANSITION; LIGANDS; TRIMERS;

AMINES;

BROMOBIMANE; CYSTEINE; DANSYL CHLORIDE; DEAMINASE; FLUORESCENT DYE; GLUCOSAMINE 6 PHOSPHATE DEAMINASE; UNCLASSIFIED DRUG;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; CHEMICAL MODIFICATION; CORRELATION ANALYSIS; ENZYME ACTIVE SITE; ESCHERICHIA COLI; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STEADY STATE; STRUCTURE ANALYSIS; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ALDOSE-KETOSE ISOMERASES; ALLOSTERIC SITE; BICYCLO COMPOUNDS; BINDING SITES; CYSTEINE; DANSYL COMPOUNDS; FLUORESCENT DYES; LIGANDS; MESYLATES; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI;

EID: 27944447348     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050306o     Document Type: Article

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