Article Abstract:
A low-molecular-mass penicillin binding-protein (PBP) in Pseudomonas aeruginosa has remarkable homology with the PBP7 of Escherichia coli. This is encoded by the gene pbpG. The gene has an open reading frame 936 base pair long encoding for a 34,115 kiloDalton protein which when cleaved yields low-molecular-mass penicillin binding-protein 7. The penicillin binding properties of the protein is investigated using labeled penicillin. The protein is characterized and compared with other low-molecular-mass penicillin binding-proteins.
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Article Abstract:
Research was conducted to examine the role of the phhC gene of Psudomonas aeruginosa as an aminotransferase for aromatic amino acid catabolism. Gene inactivation demonstrated that PhhC is critical for the catabolism of either L-phenylalanine or L-tyrosine. The required presence of PhhC for the catabolism of aromatic amino acids suggests a spatial orientation of PhhC that effectively specializes it for aromatic amino acid catabolism.
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Article Abstract:
The authors review the publications on tryptophan operon origin. The topics of interest include the biochemical pathway to tryptophan synthesis, gene fusion, tryptophan pathway's genomic distribution and ancestral operon retention in bacteria.
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