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Literature summary for 2.1.1.35 extracted from

  • Santi, D.V.; Hardy, L.W.
    Catalytic mechanism and inhibition of tRNA (uracil-5-)methyltransferase: Evidence for covalent catalysis (1987), Biochemistry, 26, 8599-8606.
    View publication on PubMed
Search for more literature for 2.1.1.35

Inhibitors

Inhibitors Comment Organism Structure
5-Fluorouracil substituted tRNA first-order inactivation in the presence of S-adenosyl-L-methionine, potent mechanism-based irreversible inhibition, formation of a stable covalent complex containing enzyme, FUra-tRNA and the methyl group of AdoMet; mechanism of inhibition Escherichia coli
p-chloromercuribenzoate at 2.5 mM, complete inhibition, completely reversed by addition of 5 mM dithiothreitol Escherichia coli
S-adenosyl-L-homocysteine product inhibition, inhibits both methylation and H-exchange reaction Escherichia coli
structural analogues of S-adenosyl-L-homocysteine nitrogen analogue of S-adenosyl-L-methionine AdoMDB inhibits at high concentrations methylation but increases H-exchange reaction Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
 x * 41000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + uridine54 in tRNA Escherichia coli tRNA modifying enzyme S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA Escherichia coli GB-1-5-39 / pTN102 tRNA modifying enzyme S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli GB-1-5-39 / pTN102
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA catalytic mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0034
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme also catalyzes an S-adenosyl-L-methionine-independent exchange reaction between [5-3H]-Urd-labeled substrate tRNA and protons of water at 1% of the normal methylation reaction rate, mechanism Escherichia coli additional information
-
 ?
additional information enzyme also catalyzes an S-adenosyl-L-methionine-independent exchange reaction between [5-3H]-Urd-labeled substrate tRNA and protons of water at 1% of the normal methylation reaction rate, mechanism Escherichia coli GB-1-5-39 / pTN102 additional information
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA 5-methylation of U in the TPsiC-loop Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: m5U-deficient tRNA from E. coli GB1-5-39 Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA tRNA modifying enzyme Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA 5-methylation of U in the TPsiC-loop Escherichia coli GB-1-5-39 / pTN102 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: m5U-deficient tRNA from E. coli GB1-5-39 Escherichia coli GB-1-5-39 / pTN102 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?
S-adenosyl-L-methionine + uridine54 in tRNA tRNA modifying enzyme Escherichia coli GB-1-5-39 / pTN102 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?

Subunits

Subunits Comment Organism
? x * 41000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Escherichia coli