2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase

This is an abbreviated version!
For detailed information about tRNA (carboxymethyluridine34-5-O)-methyltransferase, go to the full flat file.

Reaction

Synonyms

ABH8, ALKBH8, CmoA, MnmC, Trm9, Trm9-Trm112, Trm9p, TrmC, tRNA methyltransferase 9, YfcK, YML014w

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.229 tRNA (carboxymethyluridine34-5-O)-methyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
3	Activating Compound
929	AA Sequence
1	Application
8	Cloned(Commentary)
7	Cofactor
4	Crystallization (Commentary)
1	Expression
27	General Information
1	Metals/Ions
1	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
14	Organism
2	Pathway
2	pH Optimum
1	Protein Variants
8	Purification (Commentary)
5	Reaction
14	Reference
1	Source Tissue
27	Substrates and Products (Substrate)
8	Subunits
23	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 2.1.1.229 - tRNA (carboxymethyluridine34-5-O)-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme in complex with cofactors S-adenosyl-L-methionine and FAD, sitting drop vapor diffusion method, 21°C, by mixing 0.001 ml of 10 mg/ml protein with 0.001 ml of reservoir solution containing 1.8 M tri-ammonium citrate, pH 7.0 and 0.5% ethyl acetate, X-ray diffraction structure determination and analysis at 2.3 A resolution

Escherichia coli

-

735868

purified MnmC containing FAD, sitting drop method, the optimal reservoir solution contains 100 mM Bis-Tris, pH 5.5, containing 25% w/v PEG3350, 250 mM ammonium sulfate, and 10 mM hexamine cobalt(III) chloride, 5 days, X-ray diffraction structure determination and analysis at 3.0 A resolution

Escherichia coli

P77182

720990

purified recombinant detagged enzyme, sitting drop vapour diffusion method, mixing of 100 nl of 20 mg/ml protein in 200 mM NaCl, and 20 mM Tris, pH 7.5, with 100 nl of precipitation solution containing 0.3 M diethylene glycol, 0.3 M triethylene glycol, 0.3 M tetraethylene glycol, 0.3 M pentaethylene glycol, 0.1 M MOPS/HEPES-Na, pH 7.5, 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% w/v MPD, 5 h, X-ray diffraction structure determination and analysis at 1.73 A resolution, molecular replacement using the structure of Haemophilus influenzae YecO, PDB ID 1im8, chain B

Escherichia coli

P76290

735357

purified enzyme in complex with cofactors S-adenosyl-L-methionine and FAD or in complex with FAD alone, sitting drop vapor diffusion method, 21°C, by mixing 0.001 ml of 10 mg/ml protein with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.0, and 30% v/v Jeffamine ED-2001 reagent, X-ray diffraction structure determination and analysis at 2.3 A resolution

Yersinia pestis

Q8ZD36

735869