Abstract
3-Ketovalidoxylamine A C-N lyase is one of three key enzymes in the production of valienamine, which is a potent glucosidase inhibitor from validamycin A. N-p-Nitrophenyl-3-ketovalidamine, used as the substrate of 3-ketovalidoxylamine A C-N lyase, was prepared from N-p-nitrophenylvalidamine with free cells of Stenotrophomonas maltrophilia CCTCC M 204024. The yield and selectivity of N-p-nitrophenyl-3-ketovalidamine from cells were improved by treatment with 10 mM ethylenediaminetetraacetic acid. The optimal pH and temperature for N-p-nitrophenyl-3-ketovalidamine formation was pH 6.0 and 30 degrees C, respectively. N-p-Nitrophenyl-3-ketovalidamine was formed with a yield of 0.68 in the first batch.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Carbon-Nitrogen Lyases / metabolism*
-
Cyclohexenes / chemistry
-
Cyclohexenes / metabolism
-
Edetic Acid / pharmacology
-
Hexosamines / chemistry
-
Hexosamines / metabolism
-
Hydrogen-Ion Concentration
-
Inositol / analogs & derivatives
-
Inositol / chemistry
-
Inositol / metabolism
-
Kinetics
-
Models, Chemical
-
Molecular Structure
-
Nitrophenols / chemistry
-
Nitrophenols / metabolism*
-
Stenotrophomonas / drug effects
-
Stenotrophomonas / metabolism*
-
Substrate Specificity
-
Temperature
Substances
-
Cyclohexenes
-
Hexosamines
-
N-p-nitrophenyl-3-ketovalidamine
-
Nitrophenols
-
valienamine
-
Inositol
-
validamycins
-
Edetic Acid
-
Carbon-Nitrogen Lyases
-
3-ketovalidoxylamine A C-N lyase