Description

Amidases, a member of nitrilase superfamily, catalyzes the hydrolysis of an amide, leading to the formation of carboxylic acid and ammonia. Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence, and play a role in important metabolic processes[1]. –Applications-Metabolism-protein/nucleotide metabolism-Formula-N/A-Citation–References-[1]Weber BW, et al. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J Biol Chem. 2013 Oct 4;288(40):28514-23.|[2]Li W, et al. An Amidase Contributes to Full Virulence of Sclerotinia sclerotiorum. Int J Mol Sci. 2022 Sep 23;23(19):11207.|[3]Weber BW,et.al. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J Biol Chem. 2013 Oct 4;288(40):28514-23.-CASNumber-9012-56-0-MolecularWeight-N/A-Compound Purity–SMILES-[Amidase]-Research_Area-Metabolic Disease-Solubility-10 mM in DMSO-Target-Endogenous Metabolite-Isoform–Pathway-Metabolic Enzyme/Protease-MCE Product type-Enzyme