[Detection of C-P-lyase activity in a cell-free extract of Escherichia coli].
A system has been developed for in vitro testing of E. coli C-P-lyase (the enzyme cleaving C-P bonds in phosphonates). NADH, ATP, and the system of ATP regeneration were necessary but not sufficient for expression of the C-P-lyase activity in cell-free extracts of E. coli. Experimental evidence suggests that glucose 6-phosphate and (or) glucose activate C-P-lyase, serving as precursors in the formation of (alkylphosphono)ribose, an intermediate in the reaction. Guanine is the most likely acceptor of the phosphate group.
Kononova
S V
SV
Trutko
S M
SM
Laurinavichius
K S
KS
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D005947:Glucose / Q000378:metabolism; D019298:Glucose-6-Phosphate / Q000378:metabolism; D006147:Guanine / Q000378:metabolism; D008190:Lyases / Q000378:metabolism*; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D012266:Ribose / Q000031:analogs & derivatives / Q000378:metabolism
D001426:Bacterial Proteins; D009943:Organophosphorus Compounds; D009243:NAD; C032627:methylphosphonic acid; D019298:Glucose-6-Phosphate; D006147:Guanine; D012266:Ribose; D000255:Adenosine Triphosphate; D008190:Lyases; C051328:carbon-phosphorus lyase; D005947:Glucose