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Multiple active site histidine protonation states in Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE) detected by REDOR NMR
Cloning
and transcriptional analysis of Crepis alpina fatty acid desaturases
affecting the biosynthesis of crepenynic acid. N5-CAIR
mutase: Role of a CO2 binding site and substrate movement
in catalysis. Atomic-resolution
crystal structure of thioredoxin from the acidophilic bacterium Acetobacter
aceti. Alanine racemase
from the acidophile Acetobacter aceti. Structure
of a NADH-insensitive hexameric citrate synthase that resists acid
inactivation Biochemical
and structural studies of N5-carboxyaminoimidazole
ribonucleotide mutase from the acidophilic bacterium Acetobacter
aceti. Acidophilic
adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole
ribonucleotide mutase (PurE). Altered
pathway routing in a class of Salmonella enterica serovar Typhimurium mutants
defective in aminoimidazole ribonucleotide synthetase. Modular
evolution of the purine biosynthetic pathway. Lipases provide
a new mechanistic model for polyhydroxybutyrate (PHB) synthases:
Characterization of the functional residues in Chromatium vinosum PHB
synthase. Three-dimensional
structure of N5-carboxyaminoimidazole ribonucleotide
synthetase: A member of the ATP grasp protein superfamily. Crystal
structure of Escherichia coli PurE, an unusual mutase in the
purine biosynthetic pathway. X-ray
crystal structure of aminoimidazole ribonucleotide synthetase (PurM),
from the Escherichia coli purine biosynthetic pathway at 2.5 Å resolution. Investigation
of the ATP binding site of Escherichia coli aminoimidazole ribonucleotide
synthetase using affinity labeling and site-directed mutagenesis. Evidence
for the direct transfer of the carboxylate of N5-carboxyaminoimidazole
ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole
ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR
mutase. Kinetic
and structural investigations of channeling in the purine biosynthetic
pathway. X-ray
crystal structure of glycinamide ribonucleotide synthetase from Escherichia
coli. Spectroscopic
characterization of the catalytically competent ferrous site of the
resting, activated, and substrate-bound forms of phenylalanine hydroxylase. Pterin-dependent
amino acid hydroxylases. Spectroscopic
and kinetic properties of unphosphorylated rat hepatic phenylalanine
hydroxylase expressed in Escherichia coli. Comparison of resting
and activated states. Solubilization,
cellular uptake, and activity of beta-carotene and other carotenoids
as inhibitors of neoplastic transformation in cultured cells. Diverse
carotenoids protect against chemically-induced neoplastic transformation.
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