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PROSITE documentation PDOC00960 [for PROSITE entry PS01247]

Inosine-uridine preferring nucleoside hydrolase family signature





Description

Inosine-uridine preferring nucleoside hydrolase (EC 3.2.2.1) (IU-nucleoside hydrolase or IUNH) is an enzyme first identified in protozoan [1] that catalyzes the hydrolysis of all of the commonly occuring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates. This enzyme is important for these parasitic organisms, which are deficient in de novo synthsis of purines, to salvage the host purine nucleosides.

IUNH from Crithidia fasciculata has been sequenced and characterized, it is an homotetrameric enzyme of subunits of 34 Kd. An histidine has been shown to be important for the catalytic mechanism, it acts a proton donor to activate the hypoxanthine leaving group.

IUNH is evolutionary related to a number of uncharacterized proteins from various biological sources, notably:

  • Escherichia coli hypothetical protein yaaF.
  • Escherichia coli hypothetical protein ybeK.
  • Escherichia coli hypothetical protein yeiK.
  • Fission yeast hypothetical protein SpAC17G8.02.
  • Yeast hypothetical protein YDR400w.
  • An hypothetical protein from the archaebacteria Desulfurolobus ambivalens.

As a signature pattern for these proteins, we selected a highly conserved region located in the N-terminal extremity. This region contains four conserved aspartates that have been shown [2] to be located in the active site cavity.

Last update:

November 1997 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

IUNH, PS01247; Inosine-uridine preferring nucleoside hydrolase family signature  (PATTERN)


References

1AuthorsGopaul D.N. Meyer S.L. Degano M. Sacchettini J.C. Schramm V.L.
TitleInosine-uridine nucleoside hydrolase from Crithidia fasciculata. Genetic characterization, crystallization, and identification of histidine 241 as a catalytic site residue.
SourceBiochemistry 35:5963-5970(1996).
PubMed ID8634237
DOI10.1021/bi952998u

2AuthorsDegano M. Gopaul D.N. Scapin G. Schramm V.L. Sacchettini J.C.
TitleThree-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata.
SourceBiochemistry 35:5971-5981(1996).
PubMed ID8634238
DOI10.1021/bi952999m



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