KEGG   ENZYME: 1.14.14.22
Entry
EC 1.14.14.22               Enzyme                                 

Name
dibenzothiophene sulfone monooxygenase;
dszA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
dibenzothiophene-5,5-dioxide,FMNH2:oxygen oxidoreductase
Reaction(IUBMB)
dibenzothiophene-5,5-dioxide + FMNH2 + NADH + O2 = 2'-hydroxybiphenyl-2-sulfinate + H2O + FMN + NAD+ + H+ (overall reaction) [RN:R11164];
(1a) dibenzothiophene-5,5-dioxide + FMNH2 + O2 = 2'-hydroxybiphenyl-2-sulfinate + FMN-N5-oxide [RN:R12538];
(1b) FMN-N5-oxide + NADH = FMN + H2O + NAD+ + H+ (spontaneous) [RN:R12539]
Reaction(KEGG)
Substrate
dibenzothiophene-5,5-dioxide [CPD:C21150];
FMNH2 [CPD:C01847];
NADH [CPD:C00004];
O2 [CPD:C00007];
FMN-N5-oxide [CPD:C22238]
Product
2'-hydroxybiphenyl-2-sulfinate [CPD:C06742];
H2O [CPD:C00001];
FMN [CPD:C00061];
NAD+ [CPD:C00003];
H+ [CPD:C00080];
FMN-N5-oxide [CPD:C22238]
Comment
This bacterial enzyme catalyses a step in the desulfurization pathway of dibenzothiophenes. The enzyme forms a two-component system with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42) encoded by the dszD gene, which also interacts with EC 1.14.14.21, dibenzothiophene monooxygenase. The flavin-N5-oxide that is formed by the enzyme reacts spontaneously with NADH to give oxidized flavin, releasing a water molecule.
History
EC 1.14.14.22 created 2016, modified 2019
Orthology
K22220  dibenzothiophene sulfone monooxygenase
Genes
MAV: MAV_3809
MYO: OEM_p100020
MGO: AFA91_16305
MABL: MMASJCM_2557
GTA: BCM27_00650
Reference
1  [PMID:9634856]
  Authors
Gray KA, Pogrebinsky OS, Mrachko GT, Xi L, Monticello DJ, Squires CH
  Title
Molecular mechanisms of biocatalytic desulfurization of fossil fuels.
  Journal
Nat Biotechnol 14:1705-9 (1996)
DOI:10.1038/nbt1296-1705
Reference
2  [PMID:16232672]
  Authors
Ohshiro T, Kojima T, Torii K, Kawasoe H, Izumi Y
  Title
Purification and characterization of dibenzothiophene (DBT) sulfone monooxygenase, an enzyme involved in DBT desulfurization, from Rhodococcus erythropolis D-1.
  Journal
J Biosci Bioeng 88:610-6 (1999)
DOI:10.1016/S1389-1723(00)87088-7
Reference
3  [PMID:16232919]
  Authors
Konishi J, Ishii Y, Onaka T, Ohta Y, Suzuki M, Maruhashi K
  Title
Purification and characterization of dibenzothiophene sulfone monooxygenase and FMN-dependent NADH oxidoreductase from the thermophilic bacterium Paenibacillus sp. strain A11-2.
  Journal
J Biosci Bioeng 90:607-13 (2000)
DOI:10.1016/S1389-1723(00)90004-5
Reference
4  [PMID:16243275]
  Authors
Ohshiro T, Ishii Y, Matsubara T, Ueda K, Izumi Y, Kino K, Kirimura K
  Title
Dibenzothiophene desulfurizing enzymes from moderately thermophilic bacterium Bacillus subtilis WU-S2B: purification, characterization and overexpression.
  Journal
J Biosci Bioeng 100:266-73 (2005)
DOI:10.1263/jbb.100.266
Reference
5  [PMID:27120486]
  Authors
Adak S, Begley TP
  Title
Dibenzothiophene Catabolism Proceeds via a Flavin-N5-oxide Intermediate.
  Journal
J Am Chem Soc 138:6424-6 (2016)
DOI:10.1021/jacs.6b00583
Reference
6  [PMID:28784589]
  Authors
Adak S, Begley TP
  Title
Flavin-N5-oxide: A new, catalytic motif in flavoenzymology.
  Journal
Arch Biochem Biophys 632:4-10 (2017)
DOI:10.1016/j.abb.2017.08.001
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.22
IUBMB Enzyme Nomenclature: 1.14.14.22
ExPASy - ENZYME nomenclature database: 1.14.14.22
BRENDA, the Enzyme Database: 1.14.14.22

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