Intersubunit cross-talk in pyridoxal 5′-phosphate synthase, coordinated by the C terminus of the synthase subunit

Journal of Biological Chemistry

Volumn 284, Issue 12, 2009, Pages 7706-7718

  Raschle, Thomas ^a,d   Speziga, Davide ^a   Kress, Wolfgang ^a   Moccand, Cyril ^b   Gehrig, Peter ^c   Amrhein, Nikolaus ^a   Weber Ban, Eilika ^a   Fitzpatrick, Teresa B ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF GENEVA   (Switzerland)

^c FUNCTIONAL GENOMICS CENTER ZURICH   (Switzerland)

^d HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; C TERMINUS; C-TERMINAL REGIONS; CATALYTIC ABILITY; COFACTOR; COOPERATIVITY; ENZYME COMPLEXES; FLUORESCENCE SPECTROPHOTOMETRY; GLUTAMINASE; HEXAMERIC RINGS; METABOLIC ENZYMES; MICHAELIS COMPLEX; PHOSPHATE BINDING; PROTEIN CHEMISTRY; PROTEIN COMPLEXES; STRUCTURAL CHARACTERIZATION; SYNTHASE; VITAMIN B-6;

AMINO ACIDS; COORDINATION REACTIONS; CROSSTALK;

ENZYMES;

GLUTAMINE; PYRIDOXAL 5 PHOSPHATE SYNTHASE; RIBOSE 5 PHOSPHATE; SYNTHETASE; TRANSCRIPTION FACTOR PDX 1; UNCLASSIFIED DRUG; AMINOTRANSFERASE; BACTERIAL PROTEIN; DEOXYXYLULOSE PHOSPHATE; DRUG DERIVATIVE; GLUTAMINASE; GLYCERALDEHYDE 3 PHOSPHATE; LIGASE; MULTIENZYME COMPLEX; PYRIDOXAL 5 PHOSPHATE; RIBOSE PHOSPHATE; RIBOSE-5-PHOSPHATE; XYLOSE;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION; BACILLUS SUBTILIS; BIOSYNTHESIS; CHEMISTRY; ENZYMOLOGY; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; SPECTROFLUOROMETRY; THERMOTOGA MARITIMA;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; GLUTAMINASE; GLYCERALDEHYDE 3-PHOSPHATE; LIGASES; MULTIENZYME COMPLEXES; PROTEIN BINDING; PYRIDOXAL PHOSPHATE; RIBOSEMONOPHOSPHATES; SPECTROMETRY, FLUORESCENCE; THERMOTOGA MARITIMA; TRANSAMINASES; XYLOSE;

EID: 65549130157     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804728200     Document Type: Article

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