Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid dy 5-dehydroquinase.
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
Protein abundance profiling of the Escherichia coli cytosol.
Purification and characterization of 3-dehydroquinase from Escherichia coli.
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Purified E. coli 3-dehydroquinase is a dimer of 29 kDa subunits with catalytic properties like the biosynthetic DHQase of the Neurospora arom enzyme.
"The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric."
Mutagenesis of active site residues in type I dehydroquinase from Escherichia coli. Stalled catalysis in a histidine to alanine mutant.
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Lys-170 forms the Schiff base and His-143 is the general base; K170A and H143A lose about 10^6-fold activity but still bind ligand.
"Substituting alanine for each shows that H146A retains full catalytic activity while H143A shows a 10(6)-fold loss of activity."
UniProtKB entry for Escherichia coli K-12 aroD (P05194)
Reviewer notes for E. coli aroD