R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase

Journal of Biological Chemistry

Volumn 280, Issue 20, 2005, Pages 19737-19745

  Iancu, Cristina V ^a   Mukund, Susmith ^a   Fromm, Herbert J ^a   Honzatko, Richard B ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CONFORMATIONS; ENZYME INHIBITION; FRUCTOSE; HYDROPHOBICITY; MUTAGENESIS;

AMP COMPLEX; FRUCTOSE,1-6-BIPHOSPHATASE; MUTANTS; QUATERNARY TRANSITIONS;

ENZYMES;

ADENOSINE PHOSPHATE; ALANINE; FRUCTOSE BISPHOSPHATASE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; TETRAMER; BACTERIAL DNA; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONCENTRATION (PARAMETERS); CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STABILITY; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; PRIORITY JOURNAL; SURFACE PROPERTY; WILD TYPE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; ELECTRICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; KINETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

ADENOSINE MONOPHOSPHATE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DNA, BACTERIAL; ELECTROSTATICS; ENZYME STABILITY; ESCHERICHIA COLI; FRUCTOSE-BISPHOSPHATASE; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 21244449172     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501011200     Document Type: Article

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