EC Number   |
General Information |
Reference |
|---|
   1.5.1.39 | evolution |
comparison of wild-type and Y118A variants of SsuE with related wild-type and mutant H126Y MsuE from Pseudomonas fluorescens (EC 1.5.1.42), overview |
765724 |
| 1.5.1.39 | evolution |
gene chuY is highly conserved in a broad range of pathogenic bacteria |
-, 741831 |
| 1.5.1.39 | evolution |
NADH: FMN oxidoreductases (FOR) are old yellow enzyme members with a (beta/alpha) 8-barrel structure and can catalyze the oxidation of NADH to NAD+ with the flavin mononucleotide (FMN) functions as the prosthetic group |
-, 764601 |
| 1.5.1.39 | evolution |
the Pden_5119 protein is closely related to the SsuE and MsuE FRs that are parts of the two-component flavin-dependent monooxygenase systems involved in oxygenolytic cleavage of alkanesulfonates into aldehyde and sulfite |
-, 765399 |
| 1.5.1.39 | malfunction |
a chuY deletion-insertion strain shows reduced survival potential compared to wild-type and complemented strains in mammalian cells |
-, 741831 |
| 1.5.1.39 | malfunction |
inactivation of the pden_5119 gene increases susceptibility to oxidative stress, decreases growth rate and increases growth yield of Paracoccus denitrificans, growth on lower alkanesulfonates as sulfur sources is not specifically influenced. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation indicate that the Pden_5119 protein is not an obligatory component in the desulfurization pathway |
-, 765399 |
| 1.5.1.39 | malfunction |
unlike wild-type SsuE, which crystallizes as a tetramer, the Tyr118 variant structures determined here all crystallize as dimers. The Pi-helices do not contribute to the dimeric assembly, and the variants show no difference at the dimeric interface compared to wild-type. While the Y118A SsuE variant clearly cannot hydrogen bond to Ala78 through the deleted hydroxyl, the Ala78-FMN hydrogen bond remains intact and the loop containing Ala78 has not shifted in conformation. The structure of the loop containing Ala78 is also maintained in the DELTA118 SsuE structure. |
765724 |
| 1.5.1.39 | more |
enzyme structure homology modeling and docking using the structure of Thermoanaerobacter pseudethanolicus strain E39 enzyme (PDB ID 3KRZ) as the template, overview. Molecular dynamic simulation |
-, 764601 |
| 1.5.1.39 | more |
the functioning of NAD(P)H:FMN-oxidoreductase (Red) from Vibrio fischeri is not affected under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin). The functioning of Red both under conditions of MMC and in diluted solutions is the same |
764553 |
| 1.5.1.39 | more |
the Pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The Pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Enzyme-substrate binding structure analysis. In the wild-type structure, a hydrogen bond forms between the Tyr118 and a carbonyl oxygen of Ala78 from the opposing dimer, which in turn hydrogen bonds to the isoalloxazine ring system of the FMN. This network is hypothesized to aid in communication between the oligomerization interface and FMN binding |
765724 |
