AMI 1, protein arginine methyltransferase inhibitor
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MW 548.5 Da, Purity 99%. Potent, selective and reversible protein arginine methyltransferase inhibitor (IC50 = 1.63 μM). ROS° scavenger with antioxidant effects (IC50 = 8.3 μM). Inhibits arginine in vitro without competing for the AdoMet binding site. Modulates nuclear receptor-regulated transcription in vivo. Cell-permeable.
View Alternative Names
75SirT1, ANM1_HUMAN, HCP 1, HMT 2, HMT1 (hnRNP methyltransferase S. cerevisiae) like 2, HMT1 hnRNP methyltransferase, HMT1 hnRNP methyltransferase like 2, HMT1 hnRNP methyltransferase like 2 (S. cerevisiae), HRMT1 L2, HST2, HST2, S. cerevisiae, homolog of, Heterogeneous nuclear ribonucleoprotein methyltransferase 1 like 2, Heterogeneous nuclear ribonucleoproteins methyltransferase like 2, Histone-arginine N-methyltransferase PRMT1, Human mRNA for suppressor for yeast mutant, Human mRNA for suppressor for yeast mutant complete cds, IR1 B4, Interferon receptor 1-bound protein 4, Mrmt 1, NAD dependent protein deacetylase sirtuin 1, NAD-dependent deacetylase sirtuin-1, OTTHUMP00000198111, OTTHUMP00000198112, Protein arginine N-methyltransferase 1, Protein arginine methyltransferase 1, R1B4, Regulatory protein SIR2 homolog 1, S. cerevisiae like 2, SIR1_HUMAN, SIR2 like 1, SIR2, S.cerevisiae, homolog-like 1, SIR2-like protein 1, SIR2ALPHA, SIR2L1, SirtT1 75 kDa fragment, Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae), Sirtuin 1, Sirtuin type 1, hSIR2, hSIRT1
- Chemical Structure
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Chemical Structure - AMI 1, protein arginine methyltransferase inhibitor (AB141472)
2D chemical structure image of ab141472, AMI 1, protein arginine methyltransferase inhibitor
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SIRT1 impacts cellular homeostasis mediating responses to nutrient availability and stress by interacting with several transcription factors. It participates in regulating metabolism inflammation and aging processes. PRMT1 on the other hand affects gene expression and signal transduction via methylation of histones and non-histone proteins. PRMT1 operates as part of protein complexes cooperating with other methyltransferases and transcriptional regulators to control cellular growth and differentiation.
Pathways
Both SIRT1 and PRMT1 integrate into critical regulatory networks. SIRT1 plays a significant role in the SIRT1/AMPK and SIRT1/NF-κB pathways modulating energy metabolism and inflammatory responses. PRMT1 contributes to the Hedgehog and estrogen signaling pathways influencing gene transcription and cellular proliferation. Through these networks SIRT1 links to AMP-activated protein kinase (AMPK) which is paramount in energy balance while PRMT1 interacts with estrogen receptors affecting hormonal regulation.
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