| Identification | Back Directory | [Name]
PYRIDINE-2,4-DICARBOXYLIC ACID MONOHYDRATE | [CAS]
207671-42-9 | [Synonyms]
LUTIDINIC ACID MONOHYDRATE PYRIDINE-2,4-DICARBOXYLIC ACID HYDRATE 2,4-PYRIDINECARBOXYLIC ACID MONOHYDRATE 2,4-PYRIDINEDICARBOXYLIC ACID MONOHYDRATE PYRIDINE-2,4-DICARBOXYLIC ACID MONOHYDRATE 2,4-Pyridinedicarboxylicacid, hydrate (1:1) 2,4-Pyridinedicarboxylic acid Monohydrate 98% | [EINECS(EC#)]
629-130-1 | [Molecular Formula]
C7H7NO5 | [MDL Number]
MFCD00149413 | [MOL File]
207671-42-9.mol | [Molecular Weight]
185.13 |
| Chemical Properties | Back Directory | [Melting point ]
246-248 °C (dec.)(lit.) | [storage temp. ]
Store at -20°C | [solubility ]
DMSO: 1.4 mg/ml; PBS (pH 7.2): 0.2 mg/ml | [form ]
A crystalline solid | [BRN ]
131631 |
| Hazard Information | Back Directory | [Description]
2,4-Pyridinedicarboxylic Acid (2,4-PDCA) is a compound that structurally mimics 2-oxoglutarate (2-OG, also known as α-ketoglutarate) and chelates zinc, thus affecting a range of enzymes. As a 2-OG mimic, it blocks the activity of 2-OG oxygenases, which include certain lysine demethylases and a variety of hydroxylases (e.g., prolyl, collagen, lysyl). 2,4-PDCA inhibits several Jumonji domain-containing lysine demethylases when used at low micromolar concentrations. Through its effects on hydroxylases, including prolyl hydroxlase 1 (IC50 = 1.5 μM), 2,4-PDCA modulates hypoxia-inducible factor turnover, collagen synthesis, and plant cell wall formation. It can inhibit zinc-dependent enzymes, like metallo-β-lactamase. 2,4-PDCA also affects and is translocated by organic anion transporters. | [storage]
Store at -20°C | [References]
[1] Y KIDANI J H. Coordination chemical studies on metalloenzymes. II. Kinetic behavior of various types of chelating agents towards bovine carbonic anhydrase.[J]. Journal of biochemistry, 1977, 81 5: 1383-1391.
[2] M KRISTIAN KOSKI. The active site of an algal prolyl 4-hydroxylase has a large structural plasticity.[J]. The Journal of Biological Chemistry, 2007: 37112-37123. DOI: 10.1074/jbc.m706554200 [3] MUKRAM M. MACKEEN. Small-Molecule-Based Inhibition of Histone Demethylation in Cells Assessed by Quantitative Mass Spectrometry[J]. Journal of Proteome Research, 2010, 9 8: 4082-4092. DOI: 10.1021/pr100269b [4] ULRIKE LEURS. Inhibitor scaffold for the histone lysine demethylase KDM4C (JMJD2C)[J]. Bioorganic & Medicinal Chemistry Letters, 2012, 22 18: Pages 5811-5813. DOI: 10.1016/j.bmcl.2012.07.091 [5] OLIVER N F KING. Quantitative high-throughput screening identifies 8-hydroxyquinolines as cell-active histone demethylase inhibitors.[J]. PLoS ONE, 2010: e15535. DOI: 10.1371/journal.pone.0015535 [6] LINE H. KRISTENSEN. Studies of H3K4me3 demethylation by KDM5B/Jarid1B/PLU1 reveals strong substrate recognition in vitro and identifies 2,4-pyridine-dicarboxylic acid as an in vitro and in cell inhibitor[J]. The FEBS journal, 2012, 279 11: 1905-1914. DOI: 10.1111/j.1742-4658.2012.08567.x [7] SHOHEI HAMADA. Design, Synthesis, Enzyme-Inhibitory Activity, and Effect on Human Cancer Cells of a Novel Series of Jumonji Domain-Containing Protein 2 Histone Demethylase Inhibitors[J]. Journal of Medicinal Chemistry, 2010, 53 15: 5629-5638. DOI: 10.1021/jm1003655 [8] L E HORSFALL. Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila.[J]. Antimicrobial Agents and Chemotherapy, 2007: 2136-2142. DOI: 10.1128/aac.00866-06 [9] YOHANNES HAGOS. α-Ketoglutarate-related inhibitors of HIF prolyl hydroxylases are substrates of renal organic anion transporters 1 (OAT1) and 4 (OAT4).[J]. Pflugers Archiv?: European journal of physiology, 2012, 464 4: 367-374. DOI: 10.1007/s00424-012-1140-9 |
|
| Company Name: |
Energy Chemical
|
| Tel: |
021-021-58432009 400-005-6266 |
| Website: |
http://www.energy-chemical.com |
| Company Name: |
BOC Sciences
|
| Tel: |
1-631-485-4226; 16314854226 |
| Website: |
https://www.bocsci.com |
| Company Name: |
Sigma-Aldrich
|
| Tel: |
021-61415566 800-8193336 |
| Website: |
https://www.sigmaaldrich.cn |
| Company Name: |
BOC Sciences
|
| Tel: |
16314854226 |
| Website: |
www.bocsci.com |
|