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Title: Enzymology of the P-C bond. A study of the biosynthesis and biodegradation of 2-aminoethylphosphonate

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6126096

The mechanisms by which phosphorus-carbon bonds are made and are broken in biological systems are not well understood. In their laboratory they have examined the biosynthesis and biodegradation of the most predominate phosphonate in nature, 2-aminoethylphosphonate (AEP). In Bacillus cereus AEP is first converted to phosphonoacetaldehyde (PA) before hydrolysis of the P-C linkage takes place. They have examined the catalytic mechanism of the enzyme which catalyzes this hydrolysis, phosphonoacetaldehyde hydrolase (phosphonatase). Treatment of the enzyme with (/sup 3/H)-PA and NaBH/sub 4/ resulted in ethylation of an active site lysine and loss of catalytic activity. Thus, hydrolysis appears to occur via a covalent imine intermediate. Their studies of AEP biosynthesis in Tetrahymena pyriformis have focused on testing the precursor roles of PEP, phosphonopyruvate and PA. Resuspended microsomes were found to catalyze in the presence of pyridoxal phosphate and alanine, the conversion of these three precursors to AEP. The P-C bond appears to be formed by rearrangement of PEP.

Research Organization:
Univ. of Maryland, College Park
OSTI ID:
6126096
Report Number(s):
CONF-870644-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
Country of Publication:
United States
Language:
English