VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
13.
PYD2 encodes 5,6-dihydropyrimidine amidohydrolase, which participates in a novel fungal catabolic pathway
Gojković, Zoran ...
Most fungi cannot use pyrimidines or their degradation products as the sole nitrogen source. Previously, we screened several yeasts for their ability to catabolise pyrimidines. One of them, ...Saccharomyces kluyveri, was able to degrade the majority of pyrimidines. Here, a series of molecular techniques have been modified to clone pyrimidine catabolic genes, study their expressionand purify the corresponding enzymes from this yeast. The pyd2-1 mutant, which lacked the 5,6-dihydropyrimidine amidohydrolase (DHPase) activity, was transformed with wild-type S. kluyveri genomic library. The complementing plasmid contained the full sequence of the PYD2 gene, which exhibited a high level of homology with mammalian DHPases and bacterial hydantoinases. The organisation of PYD2 showed a couple of specific features.The 542-codons open reading frame was interrupted by a 63 bp intron, which does not contain the Saccharomyces cerevisiae branch-point sequence, and the transcripts contained a long 5' untranslated leader with five or six AUG codons. The derived amino acid sequence showed similarities with dihydroorotases, allantoinases and uricases from various organisms. Surprisingly, the URA4 gene from S. cerevisiae, which encodes dihydroorotase, shows greater similarity to PYD2 and other catabolic enzymes than to dihydroorotases from several other non-fungal organisms. The S. kluyveri DHPase was purified to homogeneity and sequencing of the N-terminal region revealed that the purified enzyme corresponds to the PYD2 gene product. The enzyme is a tetramer, likely consisting of similar if not identical subunits each with a molecular mass of 59 kDa. The S. kluyveri DHPase was capable of catalysing both dihydrouracil and dihydrothymine degradation, presumably by the same reaction mechanism as that described for mammalian DHPase. (Abstract truncated at 2000 characters)
Bibliografsko gradivo je bilo uspešno dodano na polico.
Dodajanje bibliografskega gradiva na polico ni uspelo.
Gradivo je že na polici.
Trajna povezava
URL:
Faktor vpliva
Dostop do baze podatkov JCR je dovoljen samo uporabnikom iz Slovenije. Vaš trenutni IP-naslov ni na seznamu dovoljenih za dostop, zato je potrebna avtentikacija z ustreznim računom AAI.
Leto
Faktor vpliva
Izdaja
Kategorija
Razvrstitev
JCR
SNIP
JCR
SNIP
JCR
SNIP
JCR
SNIP
Izberite knjižnično izkaznico:
Baze podatkov,
v katerih je revija indeksirana
Ime baze podatkov
Področje
Leto
Povezave do osebnih bibliografij avtorjev
Povezave do podatkov o raziskovalcih v sistemu SICRIS
Storitev za pridobivanje naslova trenutno ni dostopna, prosimo, poskusite še enkrat.
S klikom na gumb "V redu" boste potrdili zgoraj izbrano prevzemno mesto in dokončali postopek rezervacije.
S klikom na gumb "V redu" boste potrdili zgoraj izbrano prevzemno mesto in naslov za dostavo ter dokončali postopek rezervacije.
S klikom na gumb "V redu" boste potrdili zgoraj izbrani naslov za dostavo in dokončali postopek rezervacije.
Obvestilo
Trenutno je storitev za avtomatsko prijavo in rezervacijo nedostopna. Gradivo lahko rezervirate sami na portalu Biblos ali ponovno poskusite tukaj kasneje.
Citiranje
Funkcionalnost trenutno ni na voljo. Prosimo, poskusite kasneje.
