CAS 62037-45-0

Ac-Ala-Ala-Pro-Ala-AMC

Description:

Ac-Ala-Ala-Pro-Ala-AMC, also known as Acetyl-Alanine-Alanine-Proline-Alanine-AMC, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteases and enzyme activity. This compound features an acetyl group at the N-terminus, which enhances its stability and solubility in aqueous solutions. The sequence consists of four amino acids: alanine and proline, which contribute to its structural properties and interactions with enzymes. The AMC (7-amino-4-methylcoumarin) moiety serves as a fluorescent reporter, allowing for the detection of enzymatic cleavage and activity through fluorescence measurements. This peptide is often utilized in assays to monitor proteolytic activity, as the release of AMC upon cleavage can be quantitatively measured. Its characteristics, including solubility, stability, and fluorescence properties, make it a valuable tool in biochemical and pharmaceutical research for understanding enzyme kinetics and substrate specificity.

Formula: C₂₆H₃₃N₅O₇

InChI: InChI=1/C26H33N5O7/c1-13-11-22(33)38-21-12-18(8-9-19(13)21)28-15(3)24(35)30-25(36)20-7-6-10-31(20)26(37)16(4)29-23(34)14(2)27-17(5)32/h8-9,11-12,14-16,20,28H,6-7,10H2,1-5H3,(H,27,32)(H,29,34)(H,30,35,36)/t14-,15-,16-,20-/m0/s1

SMILES: Cc1cc(=O)oc2cc(ccc12)N[C@@H](C)C(=NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)N=C([C@H](C)N=C(C)O)O)O

Synonyms:

• N-Acetyl-alanyl-alanyl-prolyl-alanyl-amidomethylcoumarin
• N-Ac-Ala-ala-pro-ala-amc
• L-Alaninamide, N-acetyl-L-alanyl-L-alanyl-L-prolyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-
• N-acetyl-L-alanyl-L-alanyl-N-{(2S)-2-[(4-methyl-2-oxo-2H-chromen-7-yl)amino]propanoyl}-L-prolinamide

Ac-Ala-Ala-Pro-Ala-AMC

CAS: 62037-45-0

Ac-Ala-Ala-Pro-Ala-AMC is a substrate for acetylcholinesterase and its structural analogues, including Ac-Ala-Glu-Phe. It has been found to be an isomerase that catalyzes the conversion of L-serine to D-serine in human cells. The enzyme displays a high resolution crystal structure with water molecules bound at the active site. The enzyme is a dimer composed of two identical monomers. The enzyme binds two substrates through hydrogen bonding interactions and then undergoes a conformational change, which releases the products as water molecules are released from the active site.

Formula: C₂₆H₃₃N₅O₇

Purity: Min. 95%

Molecular weight: 527.57 g/mol

Ref: 3D-FA110471