EC 4.2.1.1

Base Information

• Chemical Name: EC 4.2.1.1
• CAS No.: 9001-03-0
• Molecular Formula: NULL
• Molecular Weight: 0
• Hs Code.: 35079090
• Mol file: 9001-03-0.mol

Synonyms:Anhydrase;Carbonate anhydrase; Carbonate dehydratase; Carbonic acid anhydrase; Carbonicanhydrase; Carboxyanhydrase; E.C. 4.2.1.1

Chemical Property of EC 4.2.1.1

Chemical Property:

• Appearance/Colour: powder white
• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: 2-8°C
• Solubility.: deionized water: soluble, clear to slightly hazy, colorless (Dis
• Water Solubility.: Soluble in water

Purity/Quality:

98%,99%, ^*data from raw suppliers

Carbonic Anhydrase II ^*data from reagent suppliers

Safty Information:

• Pictogram(s): B
• Hazard Codes: B,Xi,T
• Statements: 36-41-40-37/38-24-20/22
• Safety Statements: 26-45-36/37/39-53

MSDS Files:

SDS file from LookChem

Useful:

• General Description: EC 4.2.1.1, also known as carbonic anhydrase (CA), is an enzyme that catalyzes the reversible hydration of carbon dioxide. The study highlights the development of Schiff base-derived sulfonamide inhibitors targeting specific CA isozymes, particularly showing modest selectivity for the membrane-bound CA IV over cytosolic CA I and II. This selectivity suggests potential for designing more targeted inhibitors with improved therapeutic profiles and reduced side effects.

Refernces

Carbonic anhydrase inhibitors. Part 43. Schiff bases derived from aromatic sulfonamides: Towards more specific inhibitors for membrane-bound versus cytosolic isozymes

10.1016/S0223-5234(97)81681-9

The study investigates the development of more specific carbonic anhydrase (CA) inhibitors, focusing on Schiff bases derived from aromatic sulfonamides. The researchers synthesized 21 new Schiff bases using sulfanilamide, homosulfanilamide, and p-aminoethyl-benzenesulfonamide as starting materials, reacting them with various substituted benzene- and heterocyclic aldehydes. These compounds were characterized and tested for their inhibitory effects on three CA isozymes: CA I, CA II, and CA IV. The results showed that several of these new Schiff bases exhibited a modest two-fold selectivity for the membrane-bound CA IV compared to the cytosolic human isozymes CA I and II. This selectivity is attributed to a decreased potency against hCA II relative to classical inhibitors. The study suggests that these compounds could potentially lead to the development of low molecular weight, isozyme-specific CA IV inhibitors, which may have improved therapeutic profiles and fewer side effects.