scholarly journals Structure and comparative analysis of the genes encoding component C of methyl coenzyme M reductase in the extremely thermophilic archaebacterium Methanothermus fervidus.

1988 ◽  
Vol 170 (10) ◽  
pp. 4718-4726 ◽  
Author(s):  
C F Weil ◽  
D S Cram ◽  
B A Sherf ◽  
J N Reeve
Keyword(s):  
Comparative Analysis ◽  
Coenzyme M ◽  
Genes Encoding ◽  
Methanothermus Fervidus ◽  
Component C ◽  
Methyl Coenzyme M Reductase

Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria

1988 ◽  
Vol 213 (2-3) ◽  
pp. 409-420 ◽  
Author(s):  
Albrecht Klein ◽  
Rudolf Allmansberger ◽  
Martin Bokranz ◽  
Sigurd Knaub ◽  
Brigitte Müller ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Methanogenic Bacteria ◽  
Coenzyme M ◽  
Genes Encoding ◽  
Methyl Coenzyme M Reductase

scholarly journals Structure and expression of the genes, mcrBDCGA, which encode the subunits of component C of methyl coenzyme M reductase in Methanococcus vannielii

1987 ◽  
Vol 84 (12) ◽  
pp. 3992-3996 ◽  
Author(s):  
D. S. Cram ◽  
B. A. Sherf ◽  
R. T. Libby ◽  
R. J. Mattaliano ◽  
K. L. Ramachandran ◽  
...  
Keyword(s):  
Coenzyme M ◽  
Component C ◽  
Methyl Coenzyme M Reductase

scholarly journals Further expansion of methane metabolism in the Archaea

2018 ◽  
Author(s):  
Yulin Wang ◽  
Zheng-Shuang Hua ◽  
Kian Mau Goh ◽  
Paul N. Evans ◽  
Lei Liu ◽  
...  
Keyword(s):  
Hot Springs ◽  
Oxidation Process ◽  
Coenzyme M ◽  
Genes Encoding ◽  
Methane Metabolism ◽  
Encoding Genes ◽  
Methyl Coenzyme M Reductase

AbstractThe recent discovery of key methane-metabolizing genes in the genomes from the archaeal phyla Bathyarchaeota and Verstraetearchaeota has expanded our understanding of the distribution of methane metabolism outside of the phylum Euryarchaeota. Here, we recovered two near-complete crenarchaeotal metagenome-assembled genomes (MAGs) from circumneutral hot springs that contain genes for methanogenesis, including the genes that encode for the key methyl-coenzyme M reductase (MCR) complex. These newly recovered archaea phylogenetically cluster with Geoarchaeota (deep lineage of archaeal order Thermoproteales), and the MCR-encoding genes clustered with the recently reported methanogens within the Verstraetearchaeota. In addition, genes encoding hydroxybutyryl-CoA dehydratase were identified in the newly recovered methanogens, indicating they might carry out the β-oxidation process. Together, our findings further expanded the methane metabolism outside the phylum Euryarchaeota.

A comparison of the methyl reductase genes and gene products

1989 ◽  
Vol 35 (1) ◽  
pp. 101-108 ◽  
Author(s):  
Clifford F. Weil ◽  
Bruce A. Sherf ◽  
John N. Reeve
Keyword(s):  
Amino Acid ◽  
Dna Sequences ◽  
Transcription Initiation ◽  
Structural Features ◽  
Methanosarcina Barkeri ◽  
Amino Acid Sequences ◽  
Gene Products ◽  
Methanothermus Fervidus ◽  
Component C ◽  
Methyl Coenzyme M Reductase

The DNA sequences encoding component C of methyl coenzyme M reductase (mcr genes) in Methanothermus fervidus, Methanobacterium thermoautotrophicum, Methanococcus vannielii, and Methanosarcina barkeri have been published. Comparisons of transcription initiation and termination sites and of the amino acid sequences of the mcr gene products are presented. Structural features conserved within the amino acid sequences are identified and a comparison of methyl reductase with other disulfide bond synthesizing enzymes is presented.Key words: archaebacterium, methanogen, methyl reductases, gene cloning, heterodisulfide synthesis.

scholarly journals Expression, Purification, and Characterization of (R)-Sulfolactate Dehydrogenase (ComC) from the Rumen MethanogenMethanobrevibacter milleraeSM9

Archaea ◽  
2017 ◽  
Vol 2017 ◽  
pp. 1-6
Author(s):  
Yanli Zhang ◽  
Linley R. Schofield ◽  
Carrie Sang ◽  
Debjit Dey ◽  
Ron S. Ronimus
Keyword(s):  
Biosynthetic Pathway ◽  
Critical Role ◽  
Reduction Reaction ◽  
Coenzyme M ◽  
Purification And Characterization ◽  
The Third ◽  
Optimal Activity ◽  
Methyl Coenzyme M Reductase

(R)-Sulfolactate dehydrogenase (EC 1.1.1.337), termed ComC, is a member of an NADH/NADPH-dependent oxidoreductase family of enzymes that catalyze the interconversion of 2-hydroxyacids into their corresponding 2-oxoacids. The ComC reaction is reversible and in the biosynthetic direction causes the conversion of (R)-sulfolactate to sulfopyruvate in the production of coenzyme M (2-mercaptoethanesulfonic acid). Coenzyme M is an essential cofactor required for the production of methane by the methyl-coenzyme M reductase complex. ComC catalyzes the third step in the first established biosynthetic pathway of coenzyme M and is also involved in methanopterin biosynthesis. In this study, ComC fromMethanobrevibacter milleraeSM9 was cloned and expressed inEscherichia coliand biochemically characterized. Sulfopyruvate was the preferred substrate using the reduction reaction, with 31% activity seen for oxaloacetate and 0.2% seen forα-ketoglutarate. Optimal activity was observed at pH 6.5. The apparentKMfor coenzyme (NADH) was 55.1 μM, and for sulfopyruvate, it was 196 μM (for sulfopyruvate theVmaxwas 93.9 μmol min−1 mg−1andkcatwas 62.8 s−1). The critical role of ComC in two separate cofactor pathways makes this enzyme a potential means of developing methanogen-specific inhibitors for controlling ruminant methane emissions which are increasingly being recognized as contributing to climate change.

Sign in / Sign up

Export Citation Format

Share Document