Aminoacylase

Base Information

• Chemical Name: Aminoacylase
• CAS No.: 9012-37-7
• Molecular Formula: C30H34Cl2N4O
• Molecular Weight: 537.52316
• Hs Code.: 35079090
• European Community (EC) Number: 232-732-3
• ChEMBL ID: CHEMBL199585
• Pharos Ligand ID: 95Z74HDQCUFB
• Mol file: 9012-37-7.mol

Synonyms:ACY1 protein, human;Acy1 protein, mouse;Acy1 protein, rat;acylamino acid amidohydrolase;acylase I;aminoacyclase 1;aminoacylase;aminoacylase 1 protein, human;aminoacylase 1, mouse;aminoacylase 1, rat;aminoacylase I;hippuricase

Chemical Property of Aminoacylase

Chemical Property:

• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: 2-8°C
• XLogP3: 7.6
• Hydrogen Bond Donor Count: 3
• Hydrogen Bond Acceptor Count: 3
• Rotatable Bond Count: 11
• Exact Mass: 536.2109671
• Heavy Atom Count: 37
• Complexity: 726

Purity/Quality:

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

Aminoacylase 1 ^*data from reagent suppliers

Safty Information:

• Pictogram(s): Xn
• Hazard Codes: Xn
• Statements: 36/37/38-42
• Safety Statements: 22-24/25-36/37-26-24

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Canonical SMILES: C1CCC2=NC3=C(C(=CC(=C3)Cl)Cl)C(=C2C1)NCCCCCCC(=O)NCCC4=CNC5=CC=CC=C54
• Description: Aminoacylase-1 (EC 3.5.1.14) is a homodimeric zinc-binding metalloenzyme. A cytosolic enzyme with a wide range of tissue expression, it cleaves acylated L-amino acids (except L-aspartate) into L-amino acids and an acyl group. L-aspartate derivatives are cleaved by aminoacylase-2 (aspartoacylase). Aminoacylase-1 is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins.
• Uses: Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids .
• Biological Functions: Aminoacylases (N-acyl-L-amino acid amidohydrolases; EC 3.5.1.14) are widely found in animals, plants and microorganisms. The primary function of these enzymes is to remove acyl residues from N-acetylated amino acids although they may also be capable of hydrolysing carboxylic acid amides to fatty acid anions and L-amino acids. Although the catalytic mechanism of aminoacylases has been known for decades, the physiological role of these enzymes is still poorly understood. Activities of a similar nature, however, have been found in certain carboxypeptidases, aminopeptidases and dipeptidases. It could be therefore suggested that aminoacylases have a role to play in protein/peptide turnover.

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