Structural and functional analysis of PUR2,5 gene encoding bifunctional enzyme of de novo purine biosynthesis in Ogataea (Hansenula) polymorpha CBS 4732T.

摘要: Abstract We describe the cloning, sequencing and functional characterization of gene PUR2,5 , involved in de novo purine biosynthesis yeast Ogataea ( Hansenula ) polymorpha . This (2369 bp) was cloned by genetic complementation adenine requiring mutation. It encodes a bifunctional enzyme 789 amino acids (85 kDa) that catalyzes second fifth steps pathway shows dual enzymatic activity – glycinamide ribotide synthetase (GARS, EC 6.3.4.13) aminoimidazole (AIRS, 6.3.3.1). Nucleotide sequence analysis revealed presence putative regulatory elements located adjacent 5′ region. Canonical motives function as binding sites for BAS1 transcription activator were found at positions (−593) (−389). The TAATTA-box (−20) to (−14) AT-rich heteroduplex 3′-non-translated compared acid OpPUR2,5p with those corresponding enzymes other species well distant organisms like bacteria Escherichia coli human Homo sapiens A successful disruption OpPUR2,5 done. :: LEU2 replacement affects both mating sporulation processes. is deposited GenBank NCBI accession no. JF967633