Literature summary for 1.14.13.236 extracted from

Moe, L.A.; McMartin, L.A.; Fox, B.G.
Component interactions and implications for complex formation in the multicomponent toluene 4-monooxygenase (2006), Biochemistry, 45, 5478-5485.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Pseudomonas mendocina

Crystallization (Commentary)

Crystallization (Comment)	Organism
fluorescence anisotropy study of the protein-protein interactions. Binding interactions are detected between T4moD and the hydroxylase component T4moH and between T4moD and the Rieske [2Fe-2S] ferredoxin component T4moC. No binding interactions are detected between T4moD and the NADH oxidoreductase component T4moF, but T4moF is able to disrupt binding between T4moC and T4moD	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	-

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Release 2023.1 (January 2023)