Literature summary for 2.7.7.8 extracted from

Matus-Ortega, M.E.; Regonesi, M.E.; Pina-Escobedo, A.; Tortora, P.; Deho, G.; Garcia-Mena, J.
The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature (2007), Biochim. Biophys. Acta, 1769, 194-203.

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Protein Variants

Protein Variants	Comment	Organism
additional information	study on the effect of specific mutations in the two RNA binding domains KH and S1. Removal of critical motifs that stabilize the hydrophobic core of each domain, as well as a complete deletion of both severely impaireds binding to RNA. all mutants are enzymatically active but display significant changes in the kinetic behaviour of both phosphorolysis and polymerization activities. Mutants do not autoregulate efficiently and are unable to complement the growth defect of a chromosomal enzmye deletion at 18°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P05055	-	-

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Release 2023.1 (January 2023)