Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:1.3.99.3 (
acyl-CoA dehydrogenase
)
1,425
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The sigma(54)-dependent transcriptional regulator SfnR is essential for the use of dimethyl sulfone (
DMSO
(2)) as a sulfur source by Pseudomonas putida DS1. SfnR binds three SfnR-binding sites (sites 1, 2 and 3) within an intergenic region of the divergently transcribed sfnAB and sfnFG gene clusters. The site 1 region, proximal to the sfnF gene, is indispensable for the expression of the sfnFG operon, which encodes components of
DMSO
(2) monooxygenase. We investigated the transcriptional regulation of the sfnAB operon and possible functions of the sfnA gene. RT-PCR analysis revealed that the sfnAB gene cluster, which is similar to homologues of the
acyl-CoA dehydrogenase
family, was transcribed as an operon, and its expression was regulated by SfnR under conditions of sulfate starvation. Deletion analyses using lacZ as a reporter demonstrated that the region up to at least -138 bp from the transcription start point of sfnA (containing sites 2 and 3) was necessary for the expression of the sfnAB operon. A growth test of the sfnA-disrupted mutant revealed the possibility that sfnA may be involved in the use of methanethiol as a sulfur source.
...
PMID:Transcriptional regulation of the sulfate-starvation-induced gene sfnA by a sigma54-dependent activator of Pseudomonas putida. 1776 52
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 (
DMSO
2
) assimilation: SfnG converts
DMSO
2
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
DMSO
2
.
...
PMID:Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation. 3175 87
