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Literature summary for 2.7.7.79 extracted from

  • Nakamura, A.; Wang, D.; Komatsu, Y.
    Molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3'-5' direction (2018), RNA, 24, 1583-1593 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.79

Cloned(Commentary)

Cloned (Comment) Organism
gene THG1, recombinant overexpression of N-terminally His6-tagged CaThg1 in Escherichia coli strain BL21 (DE3)-pRARE2 Candida albicans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis and substrate specificity. Observed rate constants (kobs) of natural NTP or GTP analogues to pppP4 complexed with T3 are measured under single turnover conditions. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73, overview Candida albicans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
p-tRNAHis + ATP + GTP + H2O Candida albicans overall reaction pGp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + GTP + H2O Candida albicans ATCC MYA-2876 overall reaction pGp-tRNAHis + AMP + 2 diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Candida albicans A0A1D8PQL3
-
-
Candida albicans ATCC MYA-2876 A0A1D8PQL3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged CaThg1 from Escherichia coli strain BL21 (DE3)-pRARE2 by nickel affinity chromatography, dialysis, and ultrafiltration Candida albicans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information kinetic analysis and substrate specificity, overview. GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation. UTP is a poor substrate. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73. No activity with ATP, 8-oxo-GTP, isoGTP, and 8-bromo-GTP instead of GTP. The activity with CTP, 2-aminopurine, 7-deaza-GTP, ITP, and UTP depends on the tRNAHIs substrate identity Candida albicans ?
-
-
additional information kinetic analysis and substrate specificity, overview. GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation. UTP is a poor substrate. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73. No activity with ATP, 8-oxo-GTP, isoGTP, and 8-bromo-GTP instead of GTP. The activity with CTP, 2-aminopurine, 7-deaza-GTP, ITP, and UTP depends on the tRNAHIs substrate identity Candida albicans ATCC MYA-2876 ?
-
-
p-tRNAHis + ATP + 2-aminopurine + H2O
-
 Candida albicans p-2-aminopurine-p-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + 2-aminopurine + H2O
-
 Candida albicans ATCC MYA-2876 p-2-aminopurine-p-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + 5'-triphosphorylated P4 + H2O pppP4, neither ATP nor CTP is incorporated onto pppP4 Candida albicans pUp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + 5'-triphosphorylated P4 + H2O pppP4, neither ATP nor CTP is incorporated onto pppP4 Candida albicans ATCC MYA-2876 pUp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + 7-deaza-GTP + H2O
-
 Candida albicans p-7-deaza-Gp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + GTP + H2O overall reaction Candida albicans pGp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + GTP + H2O overall reaction, GTP is incorporated at the -1 position opposite the highly conserved A73 residue in eukaryotic tRNAHis Candida albicans pGp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + GTP + H2O overall reaction Candida albicans ATCC MYA-2876 pGp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + GTP + H2O overall reaction, GTP is incorporated at the -1 position opposite the highly conserved A73 residue in eukaryotic tRNAHis Candida albicans ATCC MYA-2876 pGp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + ITP + H2O very high activity Candida albicans pIp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHis + ATP + UTP + H2O low activity Candida albicans pUp-tRNAHis + AMP + 2 diphosphate
-
 ?
p-tRNAHisC73 + ATP + 7-deaza-GTP + H2O T3C73 tRNAHis variant, low activity Candida albicans p-7-deaza-Gp-tRNAHisC73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisC73 + ATP + GTP + H2O T3C73 tRNAHis variant, slightly reduced activity compared to wild-type T3A73 tRNAHis Candida albicans pGp-tRNAHisC73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisC73 + ATP + ITP + H2O T3C73 tRNAHis variant, low activity Candida albicans pIp-tRNAHisC73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisG73 + ATP + CTP + H2O T3G73 tRNAHis variant, no activity with CTP and wild-type T3A73 tRNAHis Candida albicans pCp-tRNAHisG73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisG73 + ATP + GTP + H2O T3G73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis Candida albicans pGp-tRNAHisG73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisG73 + ATP + ITP + H2O T3G73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis Candida albicans pIp-tRNAHisG73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisU73 + ATP + 2-aminopurine + H2O T3U73 tRNAHis variant, activity is similar to wild-type T3A73 tRNAHis Candida albicans p-2.aminopurine-p-tRNAHisU73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisU73 + ATP + GTP + H2O T3U73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis Candida albicans pGp-tRNAHisU73 + AMP + 2 diphosphate
-
 ?
p-tRNAHisU73 + ATP + ITP + H2O T3U73 tRNAHis variant, low activity Candida albicans pIp-tRNAHisU73 + AMP + 2 diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
CaThg1
-
 Candida albicans
THG1
-
 Candida albicans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Candida albicans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kobs for several substrate analogues, overview Candida albicans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Candida albicans

Cofactor

Cofactor Comment Organism Structure
ATP GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation Candida albicans

General Information

General Information Comment Organism
additional information molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3'-5' direction Candida albicans
physiological function tRNAHis guanylyltransferase (Thg1) transfers a guanosine triphosphate (GTP) in the 3'-5' direction onto the 5'-terminal of tRNAHis, opposite adenosine at position 73 (A73). The guanosine at the -1 position (G-1) serves as an identity element for histidyl-tRNA synthetase. Construction of a two-stranded tRNAHis molecule composed of a primer and a template strand through division at the D-loop, and evaluation of the structural requirements of the incoming GTP from the incorporation efficiencies of GTP analogues into the two-piece tRNAHis. Nitrogen at position 7 and the 6-keto oxygen of the guanine base are important for G-1 addition, but the 2-amino group is not essential. Substitution of the conserved A73 in tRNAHis reveals that the G-1 addition reaction is more efficient onto the template containing the opposite A73 than onto the template with cytidine (C73) or other bases forming canonical Watson-Crick base-pairing Candida albicans