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Literature summary extracted from

  • Hori, H.
    Transfer RNA methyltransferases with a SpoU-TrmD (SPOUT) fold and their modified nucleosides in tRNA (2017), Biomolecules, 7, E23 .
    View publication on PubMedView publication on EuropePMC

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 Aquifex aeolicus
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA Escherichia coli
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA Haemophilus influenzae
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.228 Aquifex aeolicus O67463
-
-
2.1.1.228 Escherichia coli P0A873
-
-
2.1.1.228 Haemophilus influenzae A0A0D0GZF5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.228 additional information TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected Escherichia coli ?
-
-
2.1.1.228 additional information TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected Haemophilus influenzae ?
-
-
2.1.1.228 additional information TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected. The tRNA recognition mechanism of Aquifex aeolicus TrmD shows that a micro-helix RNA corresponding to the anticodon-arm is the minimal substrate for this enzyme Aquifex aeolicus ?
-
-
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
 Aquifex aeolicus S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
 Escherichia coli S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
 Haemophilus influenzae S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.228 More knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview Aquifex aeolicus
2.1.1.228 More knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview Escherichia coli
2.1.1.228 More knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview Haemophilus influenzae

Synonyms

EC Number Synonyms Comment Organism
2.1.1.228 TrmD
-
 Aquifex aeolicus
2.1.1.228 TrmD
-
 Escherichia coli
2.1.1.228 TrmD
-
 Haemophilus influenzae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.228 S-adenosyl-L-methionine
-
 Aquifex aeolicus
2.1.1.228 S-adenosyl-L-methionine
-
 Escherichia coli
2.1.1.228 S-adenosyl-L-methionine
-
 Haemophilus influenzae

General Information

EC Number General Information Comment Organism
2.1.1.228 evolution the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Aquifex aeolicus belongs to the m1G37 methyltransferases Aquifex aeolicus
2.1.1.228 evolution the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Escherichia coli belongs to the m1G37 methyltransferases Escherichia coli
2.1.1.228 evolution the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Haemophilus influenzae belongs to the m1G37 methyltransferases Haemophilus influenzae
2.1.1.228 additional information Aquifex aeolicus TrmD can methylate G37 in the A36G37 sequence, showing that purine36 is a positive determinant for the TrmD. Formation of a disulfide bond between the two subunits stabilizes the dimer structure of Aquifex aeolicus TrmD and is required for enzymatic activity at high temperatures Aquifex aeolicus
2.1.1.228 physiological function enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 Aquifex aeolicus
2.1.1.228 physiological function enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 Escherichia coli
2.1.1.228 physiological function enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 Haemophilus influenzae