Protoporphyrin IX activates the Mg dependent guanylate cyclase from rat liver plasma membranes

Lacombe, Marie−Lise; Eberentz-Lhomme, Catherine

doi:10.1016/0006-291x(83)90378-9

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P Bork Et Al1

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1987

1996

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Cited by 7 publications

(1 citation statement)

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“…Mutation experiments in this domain show that the cyclase activity is not dependent on the PPZC domain (Suzuki et al, 1990;Feger et al, 1991). However, the domain seems to be Mg'+-dependent (Lacombe & Eberentz-Lhomme, 1983), is required for Mg2+-dependent Ras-binding (Suzuki et al, 1990), and negatively regulates the catalytic domain (Feger et al, 1991). These are all features in accordance with a PP2C-like activity.…”

Section: P Bork Et Almentioning

confidence: 99%

The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues

et al. 1996

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Abstract:A thorough sequence analysis of the various members of the eukaryotic protein serinekhreonine phosphatase 2C (PP2C) family revealed the conservation of 11 motifs. These motifs could be identified in numerous other sequences, including fungal adenylate cyclases that are predicted to contain a functionally active PP2C domain, and a family of prokaryotic serine/ threonine phosphatases including SpoIIE. Phylogenetic analysis of all the proteins indicates a widespread sequence family for which a considerable number of isoenzymes can be inferred.

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Section: P Bork Et Almentioning

confidence: 99%