KEGG   ENZYME: 1.14.13.243
Entry
EC 1.14.13.243              Enzyme                                 

Name
toluene 2-monooxygenase;
tomA1/2/3/4/5 (gene names);
toluene ortho-monooxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
toluene,NADH:oxygen oxidoreductase (2,3-dihydroxylating)
Reaction(IUBMB)
(1) toluene + NADH + H+ + O2 = 2-methylphenol + NAD+ + H2O [RN:R03560];
(2) 2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O [RN:R03608]
Reaction(KEGG)
R03560 R03608
Substrate
toluene [CPD:C01455];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007];
2-methylphenol
Product
2-methylphenol;
NAD+ [CPD:C00003];
H2O [CPD:C00001];
3-methylcatechol [CPD:C02923]
Comment
The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes. It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase. The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.
History
EC 1.14.13.243 created 2019
Pathway
ec00623  Toluene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K16242  phenol/toluene 2-monooxygenase (NADH) P3/A3
K16243  phenol/toluene 2-monooxygenase (NADH) P1/A1
K16244  phenol/toluene 2-monooxygenase (NADH) P2/A2
K16245  phenol/toluene 2-monooxygenase (NADH) P4/A4
K16246  phenol/toluene 2-monooxygenase (NADH) P5/A5
Genes
XTN: FD63_01345
XGA: BI317_02355
XHR: XJ27_14155
XPH: XppCFBP6546_14175(XppCFBP6546P_14175)
XHY: FZ025_10870
BUJ: BurJV3_3926
SMZ: SMD_4063
SACZ: AOT14_35520
SRH: BAY15_3615
STEN: CCR98_20110
PSUW: WQ53_08135
PRE: PCA10_06970(dmpL) PCA10_06980(dmpM) PCA10_06990(dmpN) PCA10_07000(dmpO) PCA10_07010(dmpP)
PKC: PKB_1742(dmpL) PKB_1743 PKB_1744(dmpN) PKB_1745 PKB_1746(dmpP)
AVN: Avin_08810(dmpP) Avin_08820(dmpO) Avin_08830(dmpN) Avin_08840(dmpM) Avin_08850(dpmL) Avin_30710(lapP) Avin_30720(lapO) Avin_30730(lapN) Avin_30740(lapM) Avin_30750(lapL)
AVL: AvCA_08810(dmpP) AvCA_08820(dmpO) AvCA_08830(dmpN) AvCA_08840(dmpM) AvCA_08850(dpmL) AvCA_30710(lapP) AvCA_30720(lapO) AvCA_30730(lapN) AvCA_30740(lapM) AvCA_30750(lapL)
AVD: AvCA6_08810(dmpP) AvCA6_08820(dmpO) AvCA6_08830(dmpN) AvCA6_08840(dmpM) AvCA6_08850(dpmL) AvCA6_30710(lapP) AvCA6_30720(lapO) AvCA6_30730(lapN) AvCA6_30740(lapM) AvCA6_30750(lapL)
ACC: BDGL_000470(mphP) BDGL_000471(mphO) BDGL_000472(mphN) BDGL_000473(mphM) BDGL_000474(mphL)
AGU: AS4_16410(dsoF) AS4_16420(dsoE) AS4_16430(dsoD) AS4_16440(dsoC) AS4_16450(dsoB)
MARJ: MARI_05340(mphL) MARI_05350(dmpM) MARI_05360(tmoA) MARI_05370 MARI_05380(dmpP)
REH: H16_B0540(poxB) H16_B0541(poxC) H16_B0542(poxD) H16_B0543(poxE) H16_B0544(poxF)
CNC: CNE_2c04860(poxB) CNE_2c04870(poxC) CNE_2c04880(poxD) CNE_2c04890(poxE) CNE_2c04900(poxF)
RME: Rmet_1326(tomA5) Rmet_1327(tomA4) Rmet_1328(tomA3) Rmet_1329(tomA2) Rmet_1330(tomA1) Rmet_1782(phyE) Rmet_1783(phyD) Rmet_1784(phyC) Rmet_1785(phyB) Rmet_1786(phyA)
BCEN: DM39_4839(dmpP) DM39_4840(phO) DM39_4841(phN) DM39_4842(dmpM) DM39_4843(mphL)
BCED: DM42_4998(dmpP) DM42_4999(phO) DM42_5000(phN) DM42_5001(dmpM) DM42_5002(phL)
HPSE: HPF_01905(dmpP) HPF_01910(tbuD) HPF_01915(tmoA2) HPF_01920(dmpM) HPF_01925(mphL)
MPT: Mpe_A2280(dmpP) Mpe_A2281(dmpO) Mpe_A2282(dmpN) Mpe_A2283(dmpM) Mpe_A2284(dmpL) Mpe_A3305(dmpO) Mpe_A3306(dmpN) Mpe_A3307(dmpM) Mpe_A3308(dmpL)
AZO: azo1846(lapL) azo1847(lapM) azo1848(lapN) azo1849(lapO) azo1850(lapP) azo2439(poxF) azo2440(poxE) azo2441(poxD) azo2442(poxC) azo2443(poxB)
AAQI: AAQM_0970(dmpL) AAQM_0971(dmpM) AAQM_0972(dmpN) AAQM_0973(dmpO) AAQM_0974(dmpP)
SJP: SJA_C1-11990(tomA1) SJA_C1-12000(tomA2) SJA_C1-12010(tomA3) SJA_C1-12020(tomA4) SJA_C1-12030(tomA5)
ASOC: CB4_02441(mphL) CB4_02442(dmpM) CB4_02443(tmoA)
 » show all
Reference
1  [PMID:7578004]
  Authors
Newman LM, Wackett LP
  Title
Purification and characterization of toluene 2-monooxygenase from Burkholderia cepacia G4.
  Journal
Biochemistry 34:14066-76 (1995)
DOI:10.1021/bi00043a012
Reference
2  [PMID:9925593]
  Authors
Yeager CM, Bottomley PJ, Arp DJ, Hyman MR
  Title
Inactivation of toluene 2-monooxygenase in Burkholderia cepacia G4 by alkynes.
  Journal
Appl Environ Microbiol 65:632-9 (1999)
DOI:10.1128/AEM.65.2.632-639.1999
Reference
3  [PMID:11751810]
  Authors
Canada KA, Iwashita S, Shim H, Wood TK
  Title
Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation.
  Journal
J Bacteriol 184:344-9 (2002)
DOI:10.1128/jb.184.2.344-349.2002
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.243
IUBMB Enzyme Nomenclature: 1.14.13.243
ExPASy - ENZYME nomenclature database: 1.14.13.243
BRENDA, the Enzyme Database: 1.14.13.243

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