Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Posttranslational Modification

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 5 of 5
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.39flavoprotein - 657741, 658119, 659330
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.39glycoprotein iNOS is N-glycosylated in vitro and in vivo. Mass spectrometry studies identify Asn695 as an N-glycosylation site of murine iNOS, mapping of the iNOS N-glycosylation site. iNOS expressed by LPS- and IFN-gamma-stimulated Raw-264.7 cells can be recognized by concanavalin A (ConA). Glycosylation at Asn695 might suppress inducible nitric oxide synthase activity by disturbing electron transfer -, 763831
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.39lipoprotein in PE placentas, eNOS can be posttranslationally modified by lipid peroxidation-derived aldehydes such as malondialdehyde or as 4-oxononenal (ONE) a highly bioreactive agent, able to inhibit eNOS activity and NO production. They covalently bind to the nucleophilic sulfhydryl and primary amine groups of proteins, forming Schiff bases, Michael adducts and protein crosslinks. The modification of proteins by lipid peroxidation products (LPPs) depends on their nature, expression and conformation, oxidative stress intensity and duration, cell type, local LPP concentration, and generates various biological responses from the expression of protective and adaptive factors to protein dysfunction, inflammation, senescence and apoptosis. The presence of LPPs in PE placentas, could be indicative of their premature senescence, in agreement with the hypothesis that accelerated placental aging is involved in PE pathophysiology via oxidative stress 765745
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.39more hemoprotein 657741, 659330
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.39sumoylation isoform neuronal nitric oxide synthase is clearly a SUMO-1 target protein both in vitro and at the cellular level. SUMO-1 conjugation of neuronal nitric oxide synthase depends on Ubc9 (E2). The interaction between neuronal nitric oxide synthase and Ubc9 is facilitated by PIASxbeta (E3) and SUMO-1 is deconjugated from neuronal nitric oxide synthase by SENP1 and SENP2 724432
Results 1 - 5 of 5