KEGG ENZYME: 1.14.14.22

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) FMNH2 + O2 = FMN-N5-peroxide [RN:R12756];
(1b) dibenzothiophene-5,5-dioxide + FMN-N5-peroxide = 2'-hydroxybiphenyl-2-sulfinate + FMN-N5-oxide [RN:R12538];
(1c) FMN-N5-oxide + NADH = FMN + H2O + NAD+ + H+ (spontaneous) [RN:R12539]

Reaction(KEGG)

R11164 R12538 R12539 R12756

Substrate

dibenzothiophene-5,5-dioxide [CPD:C21150];
FMNH2 [CPD:C01847];
NADH [CPD:C00004];
O2 [CPD:C00007];
FMN-N5-peroxide [CPD:C22379];
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-peroxide [CPD:C22379];
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_10420 OEM_p100020

MBRD:

MBRA_09600

MKY:	IWGMT90018_28920

MWU:	PT015_13400

MBOK:

MBOE_20040

MFG:	K6L26_01630 K6L26_22000

MGO:	AFA91_16305

MABL:

MMASJCM_2557

GTA:	BCM27_00650

GHN:	MVF96_00635

NFC:	KG111_17835

» show all

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

Reference

7 [PMID:32066967]

Authors

Matthews A, Saleem-Batcha R, Sanders JN, Stull F, Houk KN, Teufel R.

Title

Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases.

Journal

Nat Chem Biol 16:556-563 (2020)
DOI:10.1038/s41589-020-0476-2

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

LinkDB

DBGET integrated database retrieval system