PMID:2186811
| Citation |
Duncan, K, van Heijenoort, J and Walsh, CT (1990) Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli. Biochemistry 29:2379-86 |
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| Abstract |
The Escherichia coli D-alanyl-D-alanine-adding enzyme, which catalyzes the final cytoplasmic step in the biosynthesis of the bacterial peptidoglycan precursor UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D- Ala, has been purified to homogeneity from an E. coli strain that harbors a recombinant plasmid bearing the structural gene for this enzyme, murF. The enzyme is a monomer of molecular weight 49,000, and it has a turnover number of 784 min-1 for ATP-driven amide bond formation. Experiments monitoring the fate of radiolabeled UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelate and D-trifluoroalanine proved that the preceding enzyme in the D-alanine branch pathway, D-alanine:D-alanine ligase (ADP), is capable of synthesizing fluorinated dipeptides, which the D-Ala-D-Ala-adding enzyme can then incorporate to form UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-D-++ +trifluoroAla-D- trifluoroAla. |
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| Keywords |
Amino Acid Sequence; Carboxypeptidases/isolation & purification; Carboxypeptidases/metabolism; Chromatography, Gel; Chromatography, High Pressure Liquid; Dipeptides/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Kinetics; Molecular Sequence Data; Peptide Synthases/metabolism; Serine-Type D-Ala-D-Ala Carboxypeptidase; Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid/metabolism |
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