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Literature summary for 1.14.13.236 extracted from

  • Pikus, J.D.; Studts, J.M.; Achim, C.; Kauffmann, K.E.; Muenck, E.; Steffan, R.J.; McClay, K.; Fox, B.G.
    Recombinant toluene-4-monooxygenase: catalytic and Moessbauer studies of the purified diiron and rieske components of a four-protein complex (1996), Biochemistry, 35, 9106-9119.
    View publication on PubMed
Search for more literature for 1.14.13.236

Metals/Ions

Metals/Ions Comment Organism Structure
Iron component T4MOC contains a Rieske-type iron-sulfur center Pseudomonas mendocina

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
9600
-
-
 Pseudomonas mendocina
11600
-
-
 Pseudomonas mendocina
35000
-
-
 Pseudomonas mendocina
55000
-
-
 Pseudomonas mendocina
220000
-
 diiron hydrolase T4moH, gel filtration Pseudomonas mendocina

Organism

Organism UniProt Comment Textmining
Pseudomonas mendocina Q00456 and Q00457 and Q00460 and Q00458 and Q00459 Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively, Q00458 i.e. Rieske-type ferredoxin T4MOC, Q00459 i.e. effector protein T4MOD
-
Pseudomonas mendocina KR1 Q00456 and Q00457 and Q00460 and Q00458 and Q00459 Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively, Q00458 i.e. Rieske-type ferredoxin T4MOC, Q00459 i.e. effector protein T4MOD
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
23890
-
 pH 7.5, 25°C Pseudomonas mendocina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
toluene + NADH + H+ + O2
-
 Pseudomonas mendocina 4-methylphenol + NAD+ + H2O
-
 ?
toluene + NADH + H+ + O2
-
 Pseudomonas mendocina KR1 4-methylphenol + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 11600, component T4MOD, calculated, x * 9600, component T4moB, calculated, and x * 55000, T4moh component T4moA, * 35000, T4moH component T4moE, SDS-PAGE Pseudomonas mendocina

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre component T4MOC contains a Rieske-type iron-sulfur center Pseudomonas mendocina

General Information

General Information Comment Organism
physiological function proteins required for the in Vitro reconstitution of T4MO catalytic activity are a diiron hydroxylase (T4MOH), a Rieske-type ferredoxin (T4MOC), an effector protein (T4MOD), and an NADH oxidoreductase (T4MOF). The T4MOH component is composed of the tmoA, tmoB, and tmoE gene products with quaternary structure (alpha,beta,epsilon)2. T4MOH is the hydroxylase, the NADH-dependent multiple-turnover hydroxylation activity is increased by more than 100fold in the presence of T4MOC, which mediates highly specific electron transfer between T4MOF and T4MOH. T4MOD is a 11.6 kDa monomeric protein devoid of cofactors or redox-active metal ions and is also detected as a substoichiometric consitutent of the purified T4MOH. The rate of the hydroxylation reaction can be mildly stimulated by the further addition of separately purified T4MOD to the T4MOH Pseudomonas mendocina