2.1.1.207: tRNA (cytidine34-2'-O)-methyltransferase

This is an abbreviated version!
For detailed information about tRNA (cytidine34-2'-O)-methyltransferase, go to the full flat file.

Reaction

5-carboxymethylaminomethyluridine34 in tRNALeu

5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu

Synonyms

C/U34 2-O-methyltransferase, methyltransferase yibK, Trml, tRNA (cytidine/uridine-2'O)-ribose methyltransferase L, tRNA (cytidine34/5-carboxymethylaminomethyluridine34'-O)-methyltransferase, tRNA (Um34/Cm34) methyltransferase, tRNA methyltransferase L, YibK

ECTree

2 Transferases

2.1 Transferring one-carbon groups

2.1.1 Methyltransferases

2.1.1.207 tRNA (cytidine34-2'-O)-methyltransferase

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Results	in table
25035	AA Sequence
2	Cloned(Commentary)
5	Cofactor
1	Crystallization (Commentary)
13	General Information
2	KM Value [mM]
1	Metals/Ions
4	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
6	Organism
33	PDB ID
3	pH Optimum
20	Protein Variants
2	Purification (Commentary)
2	Reaction
6	Reference
19	Substrates and Products (Substrate)
5	Subunits
15	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Turnover Number [1/s]

Molecular Weight

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Molecular Weight on EC 2.1.1.207 - tRNA (cytidine34-2'-O)-methyltransferase

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17700

x * 17700, TrmL

17726

2 * 17726, calulated from sequence

710552

19800

Escherichia coli

2 * 19800, SDS-PAGE and gel filtration, the overall structure of an EcTrmL monomer subunit is composed of six beta-strands and six alpha-helices, in the order beta1-alpha1-beta2-alpha2-alpha3-beta3-alpha4-beta4-beta5-alpha5-beta6-alpha6. EcTrmL dimer formation is essential for tRNA recognition. The residue Y142 is critical for maintaining the dimeric form of EcTrmL, which is consistent with its central position at the interface

36000

gel filtration