Disease relevance of purF

• The mothbean cDNA, although lacking most of the plastid presequence, encodes the putative propeptide and efficiently complements purine auxotrophy in an Escherichia coli purF mutant [1].
• The authors analyzed the upstream regulatory region of purF, a gene that is expressed in a minority phase that peaks at dawn (class 2 circadian phasing) in Synechococcus elongatus, to determine whether specific cis elements are responsible for this characteristic expression pattern [2].
• Site-directed mutagenesis was employed to replace cysteine 12 with phenylalanine in Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase (amidophosphoribosyltransferase) [3].

High impact information on purF

• Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses [4].
• This site contains an imperfect inverted repeat sequence that is characteristic of sites recognized by regulatory proteins and is a candidate for the purF operator [5].
• Alignment searches of GMP synthetase with two other enzymes that bind GMP, E. coli amidophosphoribosyltransferase and human hypoxanthine-guanine phosphoribosyltransferase, suggest a structurally homologous segment which may constitute a GMP binding site [6].
• Glutamine-dependent amidophosphoribosyltransferase activity was abolished as a consequence of the mutation [3].
• NH3-dependent amidophosphoribosyltransferase was utilized for de novo purine nucleotide synthesis [3].

Chemical compound and disease context of purF

• The purC(orf)QLF operon of L. lactis is transcribed in Escherichia coli, and the gene product of the purF gene, glutamine phosphoribosylpyrophosphate amidotransferase (glutamine PRPP ATase, EC 2.4.2.14), can functionally complement the E. coli purF mutant strain TX158 [7].

Biological context of purF

• The hisT gene, which encodes tRNA pseudouridine synthase I (PSUI), was isolated on a Clarke-Carbon plasmid known to contain the purF gene [8].

Associations of purF with chemical compounds

• The purF locus codes for the first enzyme, glutamine phosphoribosylpyrophosphate amidotransferase, of the purine biosynthetic pathway [9].

Analytical, diagnostic and therapeutic context of purF

• Sequence analysis showed that the insertion occurred in a gene with no previously known function which is located directly upstream of purF [10].

References