Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Christian, T.; Gamper, H.; Hou, Y.M.
    Conservation of structure and mechanism by Trm5 enzymes (2013), RNA, 19, 1192-1199.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.228 gene TRM5, recombinant expression of C-terminally His-tagged enzyme, lacking the N-terminal peptide V2LWILWRP9, in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.228 D275A site-directed mutagenesis, the mutation leads to significantly reduced activity Homo sapiens
2.1.1.228 E288A site-directed mutagenesis, the mutation at the general base position leads to highly reduced activity Homo sapiens
2.1.1.228 E394K site-directed mutagenesis, the mutation facilitates enzyme expression in Escherichia coli Homo sapiens
2.1.1.228 H289A site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity Homo sapiens
2.1.1.228 H289R site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity Homo sapiens
2.1.1.228 M261L site-directed mutagenesis, the single M261L substitution that recapitulates the archaeal residue minimizes the 27-kDa protease product upon enzyme expression in Escherichia coli, indicating improved stability Homo sapiens
2.1.1.228 M261L/T261I site-directed mutagenesis, the double M261L substitution also shows improved stability Homo sapiens
2.1.1.228 additional information structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5 Homo sapiens
2.1.1.228 T263I site-directed mutagenesis, the mutation does not affect the enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.228 additional information
-
 additional information pre-steady-state and steady-state kinetic analysis of wild-type and mutant enzymes, the rate-determining step is product release from the enzyme, kinetic isotope effect, overview Homo sapiens
2.1.1.228 0.00042
-
 S-adenosyl-L-methionine recombinant enzyme, pH 7.3, 37°C Homo sapiens
2.1.1.228 0.00047
-
 guanine37 in tRNACys recombinant enzyme, pH 7.3, 37°C Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.228 Homo sapiens Q32P41 from the KIAA 1393 plasmid; gene TRM5
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.228 recombinant C-terminally His-tagged enzyme, lacking the N-terminal peptide V2LWILWRP9, from Escherichia coli by metal ion affinity chromatography and anion exchange chromatography Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA a highly conserved aspartate residue, D275 in Homo sapiens Trm5, in the flexible loop preceding the proposed general base E288 may be involved in the induced-fit movement of the catalytic process Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNACys
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.228 TRM5
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.228 37
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.228 0.023
-
 guanine37 in tRNACys recombinant enzyme, pH 7.3, 37°C Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.228 7.1
-
-
 Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.228 6.5 9.5 pH-activity profile Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.228 S-adenosyl-L-methionine
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.1.1.228 malfunction structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5 Homo sapiens
2.1.1.228 additional information active-site structure and overall structure analysis, molecular modeling using structure PdB ID 2ZZN, overview Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.228 50
-
 guanine37 in tRNACys recombinant enzyme, pH 7.3, 37°C Homo sapiens