Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Madeline E. Rasche"'
Publikováno v:
AIMS Microbiology, Vol 5, Iss 3, Pp 186-204 (2019)
Methane-producing archaea are among a select group of microorganisms that utilize tetrahydromethanopterin (H4MPT) as a one-carbon carrier instead of tetrahydrofolate. In H4MPT biosynthesis, β-ribofuranosylaminobenzene 5’-phosphate (RFAP) synthase
Externí odkaz:
https://doaj.org/article/b99ade350e6e484d944fa71a0fe43550
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. The α-proteobacterium Methylobacterium extorquens AM1 contains a dihydromethan
Externí odkaz:
https://doaj.org/article/8413283c18864820b4ce8faf9bc3e021
Publikováno v:
Advances in Microbiology. 10:275-294
Methane production by archaea depends on tetrahydromethanopterin (H4MPT), a pterin-containing cofactor that carries one-carbon units. Two redox reactions within the nine steps of H4MPT side chain biosynthesis have been hypothesized. Biochemical assay
Publikováno v:
AIMS Microbiology. 5:186-204
Methane-producing archaea are among a select group of microorganisms that utilize tetrahydromethanopterin (H4MPT) as a one-carbon carrier instead of tetrahydrofolate. In H4MPT biosynthesis, β-ribofuranosylaminobenzene 5’-phosphate (RFAP) synthase
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Frontiers in Microbiology
Frontiers in Microbiology
Methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. The α-proteobacterium Methylobacterium extorquens AM1 contains a dihydromethan
Autor:
Saumya Jani, Madeline E. Rasche, Kevin Chiem, David L. Lin, Brooke A. Fuentes, Marcelo E. Tolmasky
Publikováno v:
MedChemComm. 7:184-189
The aminoglycoside 6′-N-acetyltransferase type Ib, AAC(6′)-Ib, confers resistance to clinically relevant aminoglycosides and is the most widely distributed enzyme among AAC(6′)-I-producing Gram-negative pathogens. An alternative to counter the
Autor:
Thomas A. Bobik, Mark A. Arbing, Madeline E. Rasche, Michael R. Sawaya, Erick J. Morales, Todd O. Yeates, Duilio Cascio, Annie Shin
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 70:1472-1479
Prior studies have indicated that MJ1099 fromMethanocaldococcus jannaschiihas roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archa
Autor:
Julien Jorda, Duilio Cascio, Thomas A. Bobik, Tzu-Chi Wang, Dan E. McNamara, Cheene Bustos, Madeline E. Rasche, Todd O. Yeates
Publikováno v:
Journal of Biological Chemistry. 289:8852-8864
Dihydromethanopterin reductase (Dmr) is a redox enzyme that plays a key role in generating tetrahydromethanopterin (H4MPT) for use in one-carbon metabolism by archaea and some bacteria. DmrB is a bacterial enzyme understood to reduce dihydromethanopt
Publikováno v:
The FASEB Journal. 30
Autor:
Kevin, Chiem, Saumya, Jani, Brooke, Fuentes, David L, Lin, Madeline E, Rasche, Marcelo E, Tolmasky
Publikováno v:
MedChemComm. 7(1)
The aminoglycoside 6’-N-acetyltransferase type Ib, AAC(6’)-Ib, confers resistance to clinically relevant aminoglycosides and is the most widely distributed enzyme among AAC(6’)-I-producing Gram-negative pathogens. An alternative to counter the