Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate.
The biosynthetic step following the phosphoenolpyruvate (PEP) phosphomutase reaction which forms a C-P bond of bialaphos was proven by the identification of phosphonopyruvate (PnPy) and phosphonoacetaldehyde (PnAA) as intermediates in the culture broth of Streptomyces hygroscopicus, a producing organism of bialaphos, and by detection of enzymatic decarboxylation of PnPy to PnAA. Purified PnPy decarboxylase turned out to require thiamine diphosphate and Mg2+ as cofactors. PnPy decarboxylase drives the unfavorable forward reaction to form PnPy catalyzed by PEP phosphomutase and is suggested to be essential to C-P compound biosynthesis.
Nakashita
H
H
Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.
Watanabe
K
K
Hara
O
O
Hidaka
T
T
Seto
H
H
D000079:Acetaldehyde / Q000031:analogs & derivatives / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D002262:Carboxy-Lyases / Q000378:metabolism*; D009943:Organophosphorus Compounds / Q000378:metabolism*; D013302:Streptomyces / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D009943:Organophosphorus Compounds; C003126:phosphonoacetaldehyde; C003122:bialaphos; D002262:Carboxy-Lyases; D000079:Acetaldehyde