Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.13.236 - toluene 4-monooxygenase

for references in articles please use BRENDA:EC1.14.13.236
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This bacterial enzyme belongs to a family of soluble diiron hydroxylases that includes toluene-, benzene-, xylene- and methane monooxygenases, phenol hydroxylases, and alkene epoxidases. The enzyme comprises a four-component complex that includes a hydroxylase, NADH-ferredoxin oxidoreductase, a Rieske-type [2Fe-2S] ferredoxin, and an effector protein.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q00459
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
toluene 4-monooxygenase, t4mod, t4moh, t4mof, toma3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TMO
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
toluene,NADH:oxygen oxidoreductase (4-hydroxylating)
This bacterial enzyme belongs to a family of soluble diiron hydroxylases that includes toluene-, benzene-, xylene- and methane monooxygenases, phenol hydroxylases, and alkene epoxidases. The enzyme comprises a four-component complex that includes a hydroxylase, NADH-ferredoxin oxidoreductase, a Rieske-type [2Fe-2S] ferredoxin, and an effector protein.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
toluene + NADH + H+ + O2
4-methylphenol + NAD+ + H2O
show the reaction diagram
-
96.2% 4-methylphenol, 1.5% 3-methylphenol, 0.9% 2-methylphenol, 1.4% benzyl alcohol
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TmoD
effector protein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.007
Toluene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 3.4
Toluene
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
470 - 1470
Toluene
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.098 - 0.116
TmoD
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
effector protein T4moD
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TMOD_PSEME
103
0
11618
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures for native T4moD and variants with either four (DELTAN4-), or 10 (DELTAN10-) residues removed from the N-terminal at 2.1-, 1.7-, and 1.9 A resolution, respectively. Alterations of the N-terminal have little influence on the folded core of the protein
solution structure of the T4moD effector protein. The secondary structure of T4moD consists of three alpha-helices and seven beta-strands arranged in an N-terminal betaalphabetabeta and a C-terminal betaalphaalphabetabetabeta domain topology. The region around Asn34 may be involved in structural aspects contributing to functional specificity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of variants with either four (DELTAN4-) seven (DELTAN7-), or 10 (DELTAN10-) residues removed from the N-terminal. Removal leads to statistically insignificant changes in kcat, KM, kcat/KM, and KI relative to the native protein. There is no significant change in the regiospecificity of toluene oxidation with any of the T4moD variants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hemmi, H.; Studts, J.M.; Chae, Y.K.; Song, J.; Markley, J.L.; Fox, B.G.
Solution structure of the toluene 4-monooxygenase effector protein (T4moD)
Biochemistry
40
3512-3524
2001
Pseudomonas mendocina (Q00459), Pseudomonas mendocina, Pseudomonas mendocina KR1 (Q00459)
Manually annotated by BRENDA team
Lountos, G.T.; Mitchell, K.H.; Studts, J.M.; Fox, B.G.; Orville, A.M.
Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein
Biochemistry
44
7131-7142
2005
Pseudomonas mendocina (Q00459)
Manually annotated by BRENDA team