AMP-insensitive fructose bisphosphatase in Escherichia coli and its consequences.
AUTOR(ES)
Sedivy, J M
RESUMO
Inhibition of fructose bisphosphatase (EC 3.1.3.11) by AMP is thought to be an important control mechanism, and, for the Escherichia coli enzyme, is the only control known. We here report on a mutant E. coli fructose bisphosphatase almost insensitive to this inhibition. The purified enzyme is normal in other respects. A strain with this enzyme instead of the wild-type enzyme grows normally in a variety of media. A strain with a very high level of the wild-type enzyme also grows normally. A strain with the very high level of mutant enzyme, however, does show growth abnormalities, but they are not clearly associated with the AMP insensitivity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=323142Documentos Relacionados
- Expression of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and its kinase domain in Escherichia coli.
- Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene.
- Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.
- Expression of the bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli.
- DNA rehybridization during PCR: the 'Cot effect' and its consequences.
