Aspartate Residue 142 Is Important for Catalysis by ADP-glucose Pyrophosphorylase from Escherichia coli

Journal of Biological Chemistry

Volumn 276, Issue 49, 2001, Pages 46319-46325

  Frueauf, Jeremiah B ^a   Ballicora, Miguel A ^a   Preiss, Jack ^a  

^a Michigan State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYSIS; CRYSTALLIZATION; MUTAGENESIS;

LIGAND BINDING;

GLUCOSE;

ALANINE; ASPARAGINE; ASPARTIC ACID; BACTERIAL ENZYME; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLUTAMIC ACID; VEGETABLE PROTEIN; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE; PRIMER DNA;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CATALYSIS; CRYSTAL STRUCTURE; EFFECTOR CELL; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME SUBSTRATE; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STATISTICAL SIGNIFICANCE; THREE DIMENSIONAL IMAGING; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN SECONDARY STRUCTURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

AMINO ACID SEQUENCE; ASPARTIC ACID; BASE SEQUENCE; CATALYSIS; DNA PRIMERS; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEOTIDYLTRANSFERASES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, U.S. GOV'T, NON-P.H.S.;

EID: 0035824612     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M107408200     Document Type: Article

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