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

Ying Liu, Xiang-Guang Meng, Jian-Mei Li, Xiao-Hong Li, and Wei-Feng Yu

Key Laboratory of Green Chemistry and Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu, 610064, China

 

E-mail: mengxgchem@163.com

Abstract: 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 (L2) surfactant was synthesized and its metallomicelles of La3+, Cu2+, Co2+, and Zn2+ 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 LaL2 has the highest catalytic activity compared with those of the transition metal micelles CuL2, CoL2, and ZnL2. 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.

Keywords: metallomicelle – glucose-1-phosphate – hydrolysis – imidazole – catalysis mechanism

Full paper is available at www.springerlink.com.

DOI: 10.2478/s11696-013-0492-8

 

Chemical Papers 68 (5) 681–688 (2014)

Wednesday, July 15, 2020

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