Hydrophobic and electronic factors in the design of dialkylglycine decarboxylase mimics.
The first functional catalytic mimic of the enzyme dialkylglycine decarboxylase is described. This system utilizes a hydrophobically modified polyethylenimine polymer, a pyridoxamine cofactor, and a 2-aryl-2-alkylglycine sacrificial amine source to convert alpha-keto acids to alpha-amino acids at biologically relevant temperatures with multiple turnovers of the pyridoxamine catalyst. The effects of hydrophobic and electronic factors in the 2,2-disubstituted sacrificial amine source and the pyridoxamine catalyst on turnover frequency and turnover number are explored.
Chruma
Jason J
JJ
Columbia University, Department of Chemistry, 3000 Broadway, New York, NY 10027, USA.
Liu
Lei
L
Zhou
Wenjun
W
Breslow
Ronald
R
D002384:Catalysis; D050841:Glycine Dehydrogenase (Decarboxylating) / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D018716:Molecular Mimicry
D050841:Glycine Dehydrogenase (Decarboxylating)