Catalyzes the desulfonation of aliphatic sulfonates. Shows highest activity with methanesulfonate. an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H+ + H2O + sulfite.
MNVFWFLPTHGDGHFLGTSQGARPVSLPYLKQVAQAADSLGYHGVLIPTGRSCEDSWVVA
SALAPLTERLRFLVAIRPGIVSPTVSARMAATLDRLSGGRLLINVVTGGDPDENRGDGIH
LGHAERYEVTDEFLRVWRRVLQGEAVDFHGKHIHVENAKALYPPLQRPYPPLYFGGSSEA
AHELAGEQVDVYLTWGEPLPAVAAKIADVRQRAARHGRTVKFGIRLHVIVRETAEEAWRA
ADRLIEHISDETIAAAQQSFARFDSEGQRRMAALHGGRRDRLEIQPNLWAGVGLVRGGAG
TALVGDPRQVAERIGEYAELGIDSFIFSGYPHLEEAYRFAELVFPLLPEPYASLAGRGLT
NLTGPFGEMIANDVLPARAGA387
| PMID | Title & Author | Abstract | Year | |
| 0 | 31753487 | Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation.Jess Soule , Andrew D Gnann , Reyaz Gonzalez , Mackenzie J Parker , Kylie C McKenna , Son V Nguyen , Ngan T Phan , Denyce K Wicht , Daniel P Dowling | Methyl sulfur compounds are a rich source of environmental sulfur for microorganisms, but their use requires redox systems. The bacterial sfn and msu operons contain two-component flavin-dependent monooxygenases for dimethylsulfone (DMSO2) assimilation: SfnG converts DMSO2 to methanesulfinate (MSI-), and MsuD converts methanesulfonate (MS-) to sulfite. However, the enzymatic oxidation of MSI- to MS- has not been demonstrated, and the function of the last enzyme of the msu operon (MsuC) is unresolved. We employed crystallographic and biochemical studies to identify the function of MsuC from Pseudomonas fluorescens. The crystal structure of MsuC adopts the acyl-CoA dehydrogenase fold with putative binding sites for flavin and MSI-, and functional assays of MsuC in the presence of its oxidoreductase MsuE, FMN, and NADH confirm the enzymatic generation of MS-. These studies reveal that MsuC converts MSI- to MS- in sulfite biosynthesis from DMSO2. | 2020 |
| 1 | 10049377 | A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa.M A Kertesz , K Schmidt-Larbig, T Wüest | When Pseudomonas aeruginosa is grown with organosulfur compounds as sulfur sources, it synthesizes a set of proteins whose synthesis is repressed in the presence of sulfate, cysteine, or thiocyanate (so-called sulfate starvation-induced proteins). The gene encoding one of these proteins, PA13, was isolated from a cosmid library of P. aeruginosa PAO1 and sequenced. It encoded a 381-amino-acid protein that was related to several reduced flavin mononucleotide (FMNH2)-dependent monooxygenases, and it was the second in an operon of three genes, which we have named msuEDC. The MsuD protein catalyzed the desulfonation of alkanesulfonates, requiring oxygen and FMNH2 for the reaction, and showed highest activity with methanesulfonate. MsuE was an NADH-dependent flavin mononucleotide (FMN) reductase, which provided reduced FMN for the MsuD enzyme. Expression of the msu operon was analyzed with a transcriptional msuD::xylE fusion and was found to be repressed in the presence of sulfate, sulfite, sulfide, or cysteine and derepressed during growth with methionine or alkanesulfonates. Growth with methanesulfonate required an intact cysB gene, and the msu operon is therefore part of the cys regulon, since sulfite utilization was found to be CysB independent in this species. Measurements of msuD::xylE expression in cysN and cysI genetic backgrounds showed that sulfate, sulfite, and sulfide or cysteine play independent roles in negatively regulating msu expression, and sulfonate utilization therefore appears to be tightly regulated. | 1999 |
Kertesz M A , Schmidtlarbig K , Wüest, Thomas. A Novel Reduced Flavin Mononucleotide-Dependent Methanesulfonate Sulfonatase Encoded by the Sulfur-Regulated msu Operon of Pseudomonas aeruginosa[J]. Journal of Bacteriology, 1999, 181(5):1464.