Suppressing the growth of Methylobacterium species without the use of toxic chemicals has been a challenging task owing to their robustness against previous antimicrobial techniques.
Takeshi Mori +4 more
doaj +1 more source
Structure of Methylene-Tetrahydromethanopterin Dehydrogenase from Methylobacterium extorquens AM1 [PDF]
NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 A resolution. The enzyme is present as a homotrimer.
Ermler, U. ; https://orcid.org/0000-0002-9583-1418 +6 more
openaire +4 more sources
Characterization of the formyltransferase from Methylobacterium extorquens AM1 [PDF]
Methylobacterium extorquens AM1 possesses a formaldehyde‐oxidation pathway that involves enzymes with high sequence identity with enzymes from methanogenic and sulfate‐reducing archaea. Here we describe the purification and characterization of formylmethanofuran–tetrahydromethanopterin formyltransferase (Ftr), which catalyzes the reversible ...
B K, Pomper, J A, Vorholt
openaire +2 more sources
Metabolic engineering of Methylobacterium extorquens AM1 for 1-butanol production. [PDF]
Butanol is a promising next generation fuel and a bulk chemical precursor. Although clostridia are the primary industrial microbes for the fermentative production of 1-butanol, alternative engineered hosts have the potential to generate 1-butanol from alternative carbon feedstocks via synthetic metabolic pathways.
Hu B, Lidstrom ME.
europepmc +4 more sources
Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1 [PDF]
An isolated 5.2-kb fragment of Methylobacterium extorquens AM1 DNA was found to contain a gene cluster involved in methylamine utilization. Analysis of polypeptides synthesized in an Escherichia coli T7 expression system showed that five genes were present.
A Y, Chistoserdov +2 more
openaire +2 more sources
The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquens [PDF]
MxaJ is a protein of unknown function encoded by mxaJ in the mxaFJGI operon. We have constructed a mxaJ mutant of M. extorquens with a deletion which does not affect transcription of downstream genes. It contained cytochrome cL (MxaG), but neither subunit of methanol dehydrogenase (MxaF and MxaI). MxaJ is probably involved in processing this enzyme. We
K, Amaratunga +3 more
openaire +3 more sources
Transcriptional analysis of pqqD and study of the regulation of pyrroloquinoline quinone biosynthesis in Methylobacterium extorquens AM1 [PDF]
Methanol dehydrogenase, the enzyme that oxidizes methanol to formaldehyde in gram-negative methylotrophs, contains the prosthetic group pyrroloquinoline quinone (PQQ).
Lidstrom, Mary E., Ramamoorthi, Roopa
core +2 more sources
Summary: Cells, from microbes to mammals, adapt their membrane lipid composition in response to environmental changes to maintain optimal properties.
Grzegorz Chwastek +7 more
doaj +1 more source
Effective use of a horizontally-transferred pathway for dichloromethane catabolism requires post–transfer refinement [PDF]
When microbes acquire new abilities through horizontal gene transfer, the genes and pathways must function under conditions with which they did not coevolve.
Bringel, Françoise +4 more
core +1 more source
Leaf-FISH : microscale imaging of bacterial taxa on phyllosphere [PDF]
© The Author(s), 2018. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Frontiers in Microbiology 8 (2018): 2669, doi:10.3389/fmicb.2017.02669.Molecular methods for microbial
Peredo, Elena L., Simmons, Sheri L.
core +11 more sources

