deiminase, protein (arginine), HL-60 PAD, hPADI2, hPADI4, hPADVI, PAD, PAD 1, PAD 2, PAD 3, PAD 4, PAD II, PAD IV, PAD type 2, PAD-4, PAD-H19, PAD-R11, PAD-R4, PAD1, PAD2, PAD3, PAD4, PAD6, PADI1, Padi2, PADI3, PADI4, peptidyl arginine deiminas 4, peptidyl arginine deiminase, peptidyl arginine deiminase 2, peptidyl-arginine deiminase, peptidylarginine deiminase, peptidylarginine deiminase 1, peptidylarginine deiminase 2, peptidylarginine deiminase 3, peptidylarginine deiminase 4, peptidylarginine deiminase 6, peptidylarginine deiminase isoform VI, peptidylarginine deiminase IV, peptidylarginine deiminase type 4, Peptidylarginine deiminase type alpha, peptidylarginine deiminase type I, peptidylarginine deiminase type II, peptidylarginine deiminase type III, peptidylarginine deiminase type VI, peptidylarginine deiminase-4, PPAD, protein arginine deiminase, protein arginine deiminase 2, protein arginine deiminase 3, protein arginine deiminase 4
protein arginine deiminases are calcium-dependent histone-modifying enzymes whose activity is dysregulated in inflammatory diseases and cancer. PAD2 functions as an estrogen receptor (ER) coactivator in breast cancer cells via the citrullination of histone tail arginine residues at ER binding sites
despite PAD2's normally inactive status, it becomes active and citrullinates cellular proteins, but only when the intracellular Ca2+ balance is upset during neurodegenerative changes. Abnormal protein citrullination by PAD2 is closely associated with the pathogenesis of neurodegenerative disorders such as Alzheimers disease and prion disease
PAD4 is involved in cellular differentiation, is a transcriptional corepressor for the estrogen receptor and p53 (deiminates the GRIP1 (glutamate receptor interacting protein 1) binding domain of p300, facilitating its interaction with GRIP1 and thus activating transcription), and is participated in NET formation. PAD4 influences gene expression through the deimination of histones H2A, H3 and H4. PAD4 downregulates the expression of p21, a cell cycle inhibitor, as well as PUMA and OKL38 (pregnancy-induced growth inhibitor), which are inducers of apoptosis. Increased PAD4 activity contributes to the onset and progression of rheumatoid arthritis
incubation of purified PAD2 and IKKgamma proteins in the presence of Ca2+ citrullinate IKKgamma. Results demonstrate that PAD2 interacts with IKKgamma and suppresses NF-kappaB activity
PAD negatively regulates enolase activity via citrullination and enolase activity is more inactive in patients with with sporadic Creutzfeldt-Jakob disease and Alzheimer's disease than in controls
PAD negatively regulates enolase activity via citrullination. Thus, PAD-mediated citrullination regulates the diverse physiological activities of enolase
the target of citrullination is histone protein (H3), not B23. Therefore the presence of PAD4 and citrullinated histone H3 in oocytes and embryos suggests a possible role for PAD4 in preimplantation embryonic development
the target of citrullination is histone protein (H3), not B23. Therefore the presence of PAD4 and citrullinated histone H3 in oocytes and embryos suggests a possible role for PAD4 in preimplantation embryonic development
during catalysis, enzyme undergoes the transformation between protonation state N (both C351 and H236 are neutral) and state I (both residues exist as a thiolate-imidazolium ion pair). State N is calculated to be more stable than state I by 8.46 kcal/mol, and state N can transform to state I via two steps of substrate-assisted proton transfer. Starting from state N, the deamination reaction corresponds to an energy barrier of 18.82 kcal/mol. The deprotonated C351 initiates the nucleophilic attack to the substrate, which is the key step for deamination reaction. Both the deprotonated D238 and H236 can act as the bases to activate the hydrolytic water, which correspond to similar energy barriers ( about 17 kcal/mol)
enzyme is important for bacterial adhesion to fungal cells. The level of binding of a Ppad mutant strain is significantly lower than that observed for the wild-type strain. The viability of Porphyromonas gingivalis cells under normoxia increases in the presence of fungal biofilm compared with the bacteria that form single-species biofilm
in fetal testes from Sox9 knockout mice, Pai2 expression is greatly reduced. Padi-/- XY mice are fertile and show no apparent reproductive anomalies. No significant difference in H3 citrullination between wildtype and Padi2-/- XY gonads is observed
phorbol 12-myristate 13-acetate-stimulated leukocytes citrullinate fibrinogen. The citrullination is markedly enhanced when ROS formation is inhibited by the NADPH oxidase inhibitor diphenyleneiodonium. Peptidylarginine deiminase released from stimulated leukocytes is unaffected by exogenously added H2O2 at concentrations up to 1000 microM
enzyme is important for bacterial adhesion to fungal cells. The level of binding of a Ppad mutant strain is significantly lower than that observed for the wild-type strain. The viability of Porphyromonas gingivalis cells under normoxia increases in the presence of fungal biofilm compared with the bacteria that form single-species biofilm
during catalysis, enzyme undergoes the transformation between protonation state N (both C351 and H236 are neutral) and state I (both residues exist as a thiolate-imidazolium ion pair). State N is calculated to be more stable than state I by 8.46 kcal/mol, and state N can transform to state I via two steps of substrate-assisted proton transfer. Starting from state N, the deamination reaction corresponds to an energy barrier of 18.82 kcal/mol. The deprotonated C351 initiates the nucleophilic attack to the substrate, which is the key step for deamination reaction. Both the deprotonated D238 and H236 can act as the bases to activate the hydrolytic water, which correspond to similar energy barriers ( about 17 kcal/mol)