Title : Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity.

Pub. Date : 2014 Jul-Aug

PMID : 24874800






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity. bis(3',5')-cyclic diguanylic acid lon peptidase 1, mitochondrial Homo sapiens
2 Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity. bis(3',5')-cyclic diguanylic acid lon peptidase 1, mitochondrial Homo sapiens
3 Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity. bis(3',5')-cyclic diguanylic acid lon peptidase 1, mitochondrial Homo sapiens
4 Inhibition of in vitro Lon activity occurred for polyP, cAMP, ppGpp, and c-di-GMP. bis(3',5')-cyclic diguanylic acid lon peptidase 1, mitochondrial Homo sapiens
5 We also demonstrated by HPLC that Lon is able to bind c-di-GMP. bis(3',5')-cyclic diguanylic acid lon peptidase 1, mitochondrial Homo sapiens