The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration . It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration [1]. It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
gene dmrA, phylogenetic analysis and tree, recombinant expression of N-terminally His6-tagged and C-terminally His4-tagged enzyme in Escherichia coli strain BL21