Efficient hydrolysis of glucose-1-phosphate catalyzed by metallomicelles with histidine residue

✍ Scribed by Liu, Ying; Meng, Xiang-Guang; Li, Jian-Mei; Li, Xiao-Hong; Yu, Wei-Feng

• Book ID: 125406632
• Publisher: Versita
• Year: 2014
• Tongue: English
• Weight: 312 KB
• Volume: 68
• Category: Article
• ISSN: 0366-6352
• DOI: 10.2478/s11696-013-0492-8

✦ Synopsis

Phosphate esters play an important role in genetic information transfer, cell signal transduction, energy transmission and metabolic processes of living beings. Efficient catalytic hydrolysis of phosphate esters is still an attractive and challenging problem. Here, a new 2-amino-N-dodecyl-3-(1H-imidazol-5-yl)propanamide (L 2 ) surfactant was synthesized and its metallomicelles of La 3+ , Cu 2+ , Co 2+ , and Zn 2+ complexes were used as mimic metalloenzymes to catalyze the hydrolysis of glucose-1-phosphate (G1P) in a buffer solution at 35 • C. The metallomicelle systems can efficiently catalyze the hydrolysis of G1P. The rare-earth metallomicelle LaL 2 has the highest catalytic activity compared with those of the transition metal micelles CuL 2 , CoL 2 , and ZnL 2 . Different association behaviors of metallomicelles and substrate G1P were proposed. The imidazole group might accelerate the hydrolysis by activating H2O associated with the metal into a metal-OH -group. A possible catalytic mechanism was also discussed.