Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus

Article Abstract:

The thermophilic bacterium Pyrococcus furiosus requires the presence of ammonia as a nitrogen donor in the synthesis of carbamoyl phosphate as compared to the use of glutamine among other microorganisms. Carbamoyl phosphatase in P. furiosus was also found to be associated with ornithine carbamoyltransferase, which may act as a complexing partner in channeling of carbamoyl phosphate. The channelling effect is posited to prevent carbamoyl phosphate from decomposing easily under the bacterium's normal living conditions of 100-102 degrees centigrade.

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Efficient conversion of 5-substituted hydantoins to D-alpha-amino acids using recombinant Escherichia coli strains

Article Abstract:

The genes for hydantoinase and carbamylase from Agrobacterium tumefasciens was cloned and inserted in Escherichia coli. The genetically engineered E. coli was then able to produce D-phenylglycine and D-para-hydroxy phenylglycine. These D-amino acids have important applications in the production of synthetic penicillins and cephalosporins. The efficiency of D-amino acid synthesis in recombinant E. coli is influenced by the order of the recombinant genes and the incubation temperature.

Escherichia coli, Genetic recombination, Bacterial transformation, Amino acids, Amino acid synthesis, Agrobacterium tumefaciens

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Characterization of the locus encoding the (Ni-Fe) sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases

Article Abstract:

A PCR/IPCR-based technique helps separate and sequence the hydBGDA genes encoding the (Ni-Fe) hydrogenase from the archaeon Pyrococcus furiosus. Sequence data suggest the tight linking and organization of the four structural gene in a single transcription unit. Two gene products, hydB and hydG, exhibits homology to the asrB- and asrA-encoded subunits of the sulfite reductase enzyme from Salmonella typhimurium.

Analysis, Microbial enzymes, Salmonella typhimurium

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