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Literature summary for 2.7.7.52 extracted from

  • Aphasizhev, R.; Aphasizheva, I.
    Terminal RNA uridylyltransferases of trypanosomes (2008), Biochim. Biophys. Acta, 1779, 270-280.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis, sequence comparison and signature motifs, overview Trypanosoma brucei
phylogenetic analysis, sequence comparison and signature motifs, overview Leishmania tarentolae

Crystallization (Commentary)

Crystallization (Comment) Organism
TUT4 in complex with UTP, X-ray diffraction structure analysis Trypanosoma brucei

Protein Variants

Protein Variants Comment Organism
additional information mutations of metal coordinating catalytic aspartic residues D66, D68 and D136, render TUT4 inactive but have no effect on UTP binding Trypanosoma brucei

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol TUT3 and TUT4 Trypanosoma brucei 5829
-
mitochondrion RET1 Leishmania tarentolae 5739
-
mitochondrion TUT1 and TUT2 Trypanosoma brucei 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
4 * 140000, TUT1 Leishmania tarentolae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Trypanosoma brucei post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview ?
-
?
additional information Leishmania tarentolae post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview ?
-
?

Organism

Organism UniProt Comment Textmining
Leishmania tarentolae
-
-
-
Trypanosoma brucei
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
trypanosomoid form
-
Trypanosoma brucei
-
trypanosomoid form
-
Leishmania tarentolae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview Trypanosoma brucei ?
-
?
additional information post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview Leishmania tarentolae ?
-
?
additional information UTP recognition mechanism, overview. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview Leishmania tarentolae ?
-
?
additional information UTP recognition mechanism, overview. UTP specificity is determined primarily by the two closely positioned carboxylic residues, D297/D421 and E300/E424, which coordinate a crucial water molecule indicated in TUT4/RET2, uracil base interactions with invariant amino acids N147, S148, Y189, D297, E300 of TUT4. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview Trypanosoma brucei ?
-
?

Subunits

Subunits Comment Organism
More in RET1, an extra 150 amino acid insertion constitutes a helix-rich domain essential for activity, the insertion is designated as middle domain, occurs at a conserved site within the catalytic domain and is found in RET1, RET2 and TUT3, but not in TUT4, analysis of Structural diversity of trypanosomal TUTases, overview Trypanosoma brucei
tetramer 4 * 140000, TUT1 Leishmania tarentolae

Synonyms

Synonyms Comment Organism
More the enzyme belongs to a large enzyme superfamily typified by DNA polymerase beta Trypanosoma brucei
More the enzyme belongs to a large enzyme superfamily typified by DNA polymerase beta Leishmania tarentolae
RET1
-
Trypanosoma brucei
RET1
-
Leishmania tarentolae
RET2
-
Trypanosoma brucei
terminal RNA uridylyltransferase
-
Trypanosoma brucei
TUT1
-
Leishmania tarentolae
TUTase
-
Trypanosoma brucei
TUTase
-
Leishmania tarentolae
TUTase 1
-
Trypanosoma brucei
TUTase 2
-
Trypanosoma brucei
TUTase 3
-
Trypanosoma brucei
TUTase 4
-
Trypanosoma brucei