Disease relevance of purF

• All of the genes in this region of the chromosome were found to be transcribed in a counter-clockwise direction on the E. coli map which revises the direction of purF transcription [1].
• The Bacillus subtilis gene encoding glutamine phosphoribosylpyrophosphate amidotransferase (amidophosphoribosyltransferase) was cloned in pBR322 [2].

High impact information on purF

• Although Arg-30, Asn-74, and Asn-79 appear totally conserved throughout the purF glutamine-dependent amidotransferases, their potential roles in catalysis and binding remain unexplored for any member of the enzyme family [3].
• A purF type glutamine amide transfer domain was identified upon inspection of the amino-terminal amino acid sequence of the asparagine synthetase B protein [4].
• A purC-lacZ fusion was constructed to monitor gene expression [5].
• This mutation abolished repression of a purF-lacZ fusion [6].
• This indicates that cells contain a greater than 100-fold excess of purR-encoded repressor than is needed to regulate the chromosomal purF operon [6].

Chemical compound and disease context of purF

• Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase [7].
• Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis [8].
• Regulation of Escherichia coli purF. Mutations that define the promoter, operator, and purine repressor gene [6].
• The Escherichia coli gene purF, coding for 5-phosphoribosylamine:glutamine pyrophosphate phosphoribosyltransferase (amidophosphoribosyltransferase) was subcloned from a ColE1-purF plasmid into pBR322 [7].
• A series of deletions was constructed in cloned Escherichia coli purF encoding glutamine phosphoribosylpyrophosphate amidotransferase [9].

Biological context of purF

• S1 nuclease analysis has demonstrated that some of these genes are part of the hisT or purF operons [1].
• The nucleotide sequence of a 2478-base pair PvuI-HinfI fragment encoding purF was determined [7].
• Sequence homology was not detected in the glutamine amide transfer domains of E. coli anthranilate synthase and amidophosphoribosyltransferase [10].

Associations of purF with chemical compounds

• Mutations in apbC block function of the APB pathway since they prevent growth of a purF mutant in the absence of thiamine [11].
• The Cys-His-Asp catalytic triad is implicated in the glutamine amide transfer function of purF-type amidotransferases [12].
• Apparent dissociation constants of 3.4 nM were determined for binding of holorepressor to purF operator and of 1.7 and 7.1 microM were determined for aporepressor interaction with guanine and hypoxanthine, respectively [13].
• Enzyme specific activity, immunological reactivity, in vitro lability to O2, Fe-S content, and NH2-terminal processing were virtually identical with amidophosphoribosyltransferase purified from B. subtilis [2].
• The NH2-terminal cysteine of amidophosphoribosyltransferase was determined to be the residue alkylated by [6-14C]DON [8].

Other interactions of purF

• A 9.7-kilobase pair segment of the Escherichia coli chromosome spanning the hisT and purF loci has been characterized [1].
• These measurements indicated 5- to 17-fold coregulation of genes purF, purHD, purC, purMN, purL, and purEK and thus confirm the existence of a pur regulon [14].
• The folC gene is located about 1 kilobase upstream of the purF gene region at 50 min on the Escherichia coli map [15].

References