A two-step process controls the formation of the bienzyme cysteine synthase complex

Journal of Biological Chemistry

Volumn 285, Issue 17, 2010, Pages 12813-12822

  Salsi, Enea ^a   Campanini, Barbara ^a   Bettati, Stefano ^a,b   Raboni, Samanta ^a   Roderick, Steven L ^c   Cook, Paul F ^d,e   Mozzarelli, Andrea ^a,b  

^a UNIVERSITY OF PARMA   (Italy)

^b NATIONAL INSTITUTE OF BIOSTRUCTURES AND BIOSYSTEMS   (Italy)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^d UNIVERSITY OF OKLAHOMA   (United States)

^e NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BIOSYNTHETIC PATHWAY; BRANCH POINTS; C-TERMINAL PEPTIDES; COMPLEX FORMATIONS; CONFORMATIONAL CHANGE; CYSTEINE SYNTHASE; ENCOUNTER COMPLEX; NITROGEN ASSIMILATION PATHWAY; PH VALUE; PHYSIOLOGICAL REGULATORS; REGULATION OF ENZYME ACTIVITY; REGULATORY COMPLEXES; SERINE ACETYLTRANSFERASE; STOPPED FLOW; TRANSIENT FORMATION; TWO-STEP MECHANISMS; TWO-STEP PROCESS;

AMINO ACIDS; CATALYSTS; ENZYME ACTIVITY; ENZYMES; FLUORESCENCE SPECTROSCOPY; LAWS AND LEGISLATION; NITROGEN FIXATION; PHOSPHATASES; PLANT SHUTDOWNS; REACTION KINETICS; SULFUR;

COMPLEXATION;

CYSTEINE; CYSTEINE SYNTHASE; SERINE ACETYLTRANSFERASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME REGULATION; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SYNTHESIS; FLUORESCENCE SPECTROSCOPY; HAEMOPHILUS INFLUENZAE; ISOMERIZATION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; TEMPERATURE SENSITIVITY;

BACTERIAL PROTEINS; CYSTEINE SYNTHASE; DISULFIDES; HAEMOPHILUS INFLUENZAE; HYDROGEN-ION CONCENTRATION; KINETICS; MULTIENZYME COMPLEXES; PLANTS; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SERINE O-ACETYLTRANSFERASE; SPECTROMETRY, FLUORESCENCE; SULFUR;

EID: 77951212184     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.075762     Document Type: Article

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