F
IPR019911

Alkanesulphonate monooxygenase, FMN-dependent

InterPro entry
Short nameAlkanesulphonate_mOase_FMN-dep
Overlapping
homologous
superfamilies
 

Description

This entry represents a distinct group of proteins within the wider luciferase-like family of monooxygenases, including SsuD from E.coli and MsuD from P.fluorescens which are closely related
[3, 1, 2]
. They catalyse the desulphonation of aliphatic sulfonates in an FMN-dependent fashion
[1, 2]
. SsuD converts alkanesulfonates to the corresponding aldehyde and sulfite in which it catalyses the C-S bond cleavage of C2-C10 alkyl-substituted sulfonates, in addition to alkyl chains with bulkier chemical groups and larger buffer molecules, whereas MsuD is most active with a C1 sulfonate in the conversion of methanesulfonate to sulfite, completing the sulfur assimilation process during sulfate starvation
[2]
.

References

1.A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa. Kertesz MA, Schmidt-Larbig K, Wuest T. J. Bacteriol. 181, 1464-73, (1999). View articlePMID: 10049377

2.Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer. Liew JJM, El Saudi IM, Nguyen SV, Wicht DK, Dowling DP. J Biol Chem 297, 100823, (2021). PMID: 34029591

3.Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. Eichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ. J. Mol. Biol. 324, 457-68, (2002). View articlePMID: 12445781

GO terms

biological process

  • None

cellular component

  • None

Cross References

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