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Literature summary for 3.4.13.9 extracted from

  • Surazynski, A.; Liu, Y.; Miltyk, W.; Phang, J.M.
    Nitric oxide regulates prolidase activity by serine/threonine phosphorylation (2005), J. Cell. Biochem., 96, 1086-1094.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
8-Br-cGMP strong and rapid stimulation of enzyme activity by phosphorylation Mus musculus
NO NO-donors such as SIN I and DETA/NO increase enzyme activity in time- and dose-dependent manner. Enzyme activity also increases upon transfection of cells with iNOS. Increased enzymic activity is accompanied by increase in serine/threonine phosphorylation of enzyme Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein increased enzymic activity after treatment with NO donors is accompanied by increase in serine/threonine phosphorylation of enzyme. 8-Br-cGMP strongly and rapidly stimulates enzyme activity by phosphorylation Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
NIH-3T3 cell fibroblast cell line Mus musculus
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