Disease relevance of PRPSAP1

• The enzyme complex was then partially reconstituted in situ by coexpression of PAP39 with PRS I or PRS II in E. coli cells [1].

High impact information on PRPSAP1

• Covalent cross-linking experiments gave definitive evidence for molecular interaction of PAP39 with the catalytic subunits [2].
• We have cloned the cDNA for the major one of 39 kDa (PAP39) from a rat liver cDNA library [2].
• The human phosphoribosylpyrophosphate synthetase-associated protein 39 gene (PRPSAP1) is located in the chromosome region 17q24-q25 [3].
• A human cDNA encoding 41-kDa phosphoribosylpyrophosphate (PRPP) synthetase (PRS)-associated protein (PAP41) was cloned from two expressed sequence tag (EST) clones having the nucleotide similarity of 61.5 and 70.0% to human PAP39 cDNA [4].
• PAP39 complexed with PRS I was more readily degraded by proteolysis than seen with PRS II, in vivo and in vitro [1].

Biological context of PRPSAP1

• Evidence indicated molecular interaction between PAP39 and the catalytic subunits and an inhibitory effect of PAP39 on the catalytic activity [5].
• Another component, PRPP synthetase-associated protein of 39 kDa (PAP39), was cloned from cDNA library of the rat liver [5].

Analytical, diagnostic and therapeutic context of PRPSAP1

• Immunoprecipitation experiments revealed that all the catalytic subunits existed as complexes containing PAP39 [2].

References