Zobrazeno 1 - 10
of 147
pro vyhledávání: '"Rowena G. Matthews"'
Autor:
Elise R Hondorp, Rowena G Matthews
Publikováno v:
PLoS Biology, Vol 2, Iss 11, p e336 (2004)
In nature, Escherichia coli are exposed to harsh and non-ideal growth environments-nutrients may be limiting, and cells are often challenged by oxidative stress. For E. coli cells confronting these realities, there appears to be a link between oxidat
Externí odkaz:
https://doaj.org/article/0562054c81ea4e27be6ee733ddc2f46e
Autor:
Rowena G. Matthews
Publikováno v:
Chemistry and Biochemistry of Flavoenzymes ISBN: 9781351070577
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74a33da472b08ea468648e31d256ed79
https://doi.org/10.1201/9781351070577-16
https://doi.org/10.1201/9781351070577-16
Publikováno v:
Proceedings of the National Academy of Sciences. 106:18527-18532
Cobalamin-dependent methionine synthase (MetH) is a modular protein that catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine to produce methionine and tetrahydrofolate. The cobalamin cofactor, which serves as both acc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7089525cf0b6689193ca74e5a3bee58
https://doi.org/10.1073/pnas.0906132106
https://doi.org/10.1073/pnas.0906132106
Autor:
Rowena G. Matthews
Publikováno v:
Journal of Biological Chemistry. 284:26217-26228
I was born in Cambridge, England, where my father, David Green, had done the research for his Ph.D. in the laboratory of Sir Frederick Gowland Hopkins and where he remained as a Beit Fellow. My mother was English, whereas my father was an American ci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9290fca346379f80761ad97966e92085
https://doi.org/10.1074/jbc.x109.041178
https://doi.org/10.1074/jbc.x109.041178
Autor:
Elise R. Hondorp, Rowena G. Matthews
Publikováno v:
Journal of Bacteriology. 191:3407-3410
Cobalamin-independent methionine synthase (MetE) catalyzes the final step in Escherichia coli methionine biosynthesis but is inactivated under oxidative conditions, triggering a methionine deficiency. This study demonstrates that the mutation of MetE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f15bff8979552b0649b31a1dd82deb6e
https://doi.org/10.1128/jb.01722-08
https://doi.org/10.1128/jb.01722-08
Publikováno v:
Current Opinion in Structural Biology. 18:658-666
Methyltransferases that employ cobalamin cofactors, or their analogs the cobamides, as intermediates in catalysis of methyl transfer play vital roles in energy generation in anaerobic unicellular organisms. In a broader range of organisms they are in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4977f8b0362ad8665128fad723223a5e
https://doi.org/10.1016/j.sbi.2008.11.005
https://doi.org/10.1016/j.sbi.2008.11.005
Publikováno v:
Journal of the American Chemical Society. 130:16374-16381
The cobalamin-dependent methionine synthase (MetH) from Escherichia coli is a modular enzyme that catalyzes a methyl group transfer from methyltetrahydrofolate to homocysteine via a methylcob(III)alamin (MeCbl) intermediate, generating tetrahydrofola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e550fecf5a55d17ab3ed89ac9d1d024c
https://doi.org/10.1021/ja8038129
https://doi.org/10.1021/ja8038129
Autor:
Katherine A. Pattridge, Sha Huang, Rowena G. Matthews, Martha L. Ludwig, Gail Romanchuk, Ian A. Wilson, Scott A. Lesley
Publikováno v:
Protein Science. 16:1588-1595
The crystal structure of the Thermotoga maritima gene product TM0269, determined as part of genome-wide structural coverage of T. maritima by the Joint Center for Structural Genomics, revealed structural homology with the fourth module of the cobalam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68dbee1d5af8b43e805b010a6291d11b
https://doi.org/10.1110/ps.072936307
https://doi.org/10.1110/ps.072936307
Publikováno v:
Biochemistry. 46:8024-8035
Cobalamin-dependent methionine synthase (MetH) of Escherichia coli is a 136 kDa, modular enzyme that undergoes large conformational changes as it uses a cobalamin cofactor as a donor or acceptor in three separate methyl transfer reactions. At differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e661f4c6641bf415c5b887aa8221a26d
https://doi.org/10.1021/bi700341y
https://doi.org/10.1021/bi700341y
Autor:
Jacalyn M. Green, Rowena G. Matthews
Publikováno v:
EcoSal Plus. 2(2)
Many microorganisms and plants possess the ability to synthesize folic acid derivatives de novo, initially forming dihydrofolate. All the folic acid derivatives that serve as recipients and donors of one-carbon units are derivatives of tetrahydrofola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::222ed7a25547ed0fe073e38eb0ac17dd
https://pubmed.ncbi.nlm.nih.gov/26443588
https://pubmed.ncbi.nlm.nih.gov/26443588