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• W2050349028 abstract "Recombinant human abacavir monophosphate deaminase (hABC-MP deaminase) was compared with the recently described rat N 6 -methyl-AMP (meAMP) aminohydrolase. hABC-MP deaminase, a 42 kDa polypeptide, exists predominantly as a monomer under non-denaturing conditions. Similar to the rat enzyme, hABC-MP deaminase efficiently catalyzes the hydrolytic deamination of natural substrates meAMP ( 5 ), N 6 , N 6 -dimethyl-AMP ( 13 ) and medAMP ( 6 ). Acyclic nucleoside phosphonate (ANP) N 6 -cyclopropyl-2,6-diamino-9-[2-(phosphonomethoxy)ethyl]purine (cPrPMEDAP) ( 1 ), an intermediate intracellular metabolite of antileukemic agent GS-9219, was effectively converted to the corresponding active guanine analog by hABC-MP deaminase. In addition to cPrPMEDAP ( 1 ), a number of other biologically active N 6 -substituted purine ANPs are alternative substrates for hABC-MP deaminase. The efficiency of their deamination depends on the character of N 6 -substitution in the adenine and/or 2,6-diaminopurine ring. ANPs with N 6 -cyclic substituents are deaminated more readily than corresponding compounds with aliphatic substituents of the same length. The deamination of ANPs is also influenced by modifications at the phosphonoalkyl side chain. Among 9-[2-(phosphonomethoxy)propyl] ANPs, ( S )-enantiomers are preferred to ( R )-enantiomers. Alternatively, the presence of extended 9-[2-(phosphonoethoxy)ethyl] moiety leads to a moderate increase in the reaction velocity compared to cPrPMEDAP ( 1 ). Comparison of hABC-MP deaminase and the rat meAMP aminohydrolase across a broad spectrum of N 6 -substituted substrates revealed a strong correlation of their substrate specificities. Similar to the rat meAMP aminohydrolase, hABC-MP deaminase was highly sensitive to deoxycoformycin monophosphate, but not to the guanine product of cPrPMEDAP ( 1 ) deamination. Together, these data demonstrate that hABC-MP deaminase is human meAMP aminohydrolase involved in the intracellular activation of biologically active N 6 -substituted nucleotide analogs." @default.
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• W2050349028 title "Human N6-Methyl-AMP/DAMP Aminohydrolase (Abacavir 5'-Monophosphate Deaminase) is Capable of Metabolizing N6-Substituted Purine Acyclic Nucleoside Phosphonates" @default.
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• W2050349028 doi "https://doi.org/10.1135/cccc20080275" @default.
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