METAPHOSPHATE SYNTHESIS BY AN ENZYME FROM ESCHERICHIA-COLI
METAPHOSPHATE SYNTHESIS BY AN ENZYME FROM ESCHERICHIA-COLI
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DOI:
10.1016/0006-3002(56)90280-3
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发表时间:
1956-01-01
期刊:
影响因子:
--
通讯作者:
SIMMS, ES
中科院分区:
文献类型:
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作者:
KORNBERG, A;KORNBERG, SR;SIMMS, ES
An enzyme that synthesizes metaphosphate was purified more than 100-fold from extracts of E. coli. The reaction may be described by the equation: [image] Only the terminal phosphate group of ATP was found in the polymer. Since ADP, the other product of the reaction, proved to be a very potent inhibitor, it is believed that an ATP-regen-erating system is generally coupled to the reaction. Inorganic pyrophosphate (PP), but not inorganic orthophosphate or adenine nucleotide, are incorporated into metaphosphate. However, lack of a requirement for PP and the absence of any inhibition by PP-ase leaves the nature of the true primer (PO3)n in doubt. The phosphate polymer is characterized as a long-chain metaphosphate because it (a) induces metachromasy, (b) forms an acid-insoluble complex with protein, (c) is nondialyzable, (d) is labile to acid and alkali, (e) binds tenaciously to anion exchange resins, and (f) is not attacked by nucleases.