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Synthesis, enzyme — substrate interaction, and herbicidal activity of phosphoryl analogues of glycine
Author(s) -
Natchev Ivan A.
Publication year - 1988
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.198819880908
Subject(s) - chemistry , substrate (aquarium) , hydrolysis , enzyme , glycine , triazine , chymotrypsin , selectivity , organic chemistry , acetylation , alkaline phosphatase , catalysis , stereochemistry , biochemistry , amino acid , trypsin , gene , geology , oceanography
The interactions of hydrophosphoryl compounds 1 – 10 and 1,3,5‐triacetylhexahydro‐1,3,5‐triazine furnish the N ‐acetylated (aminomethyl)phosphoryl compounds 11–20 , which, upon acidic hydrolysis, lead to 3, 6, 9 , and 21 – 24 . Strict selectivity is observed in the enzyme‐catalyzed hydrolysis with the enzymes α‐chymotrypsin, phosphodiesterase I, and alkaline phosphatase. Some of the synthesized materials exhibit herbicidal and antitumor activity.