Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Birgit E. Alber"'
Publikováno v:
Journal of bacteriology. 201(4)
Rhodobacter sphaeroides is able to use 3-hydroxypropionate as the sole carbon source through the reductive conversion of 3-hydroxypropionate to propionyl coenzyme A (propionyl-CoA). The ethylmalonyl-CoA pathway is not required in this process because
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26e3e69c983362781b249bb729bae010
https://pubmed.ncbi.nlm.nih.gov/30455284
https://pubmed.ncbi.nlm.nih.gov/30455284
Autor:
Michael S. Carter, Birgit E. Alber
Publikováno v:
Journal of Bacteriology. 197:3048-3056
Propionyl coenzyme A (propionyl-CoA) assimilation by Rhodobacter sphaeroides proceeds via the methylmalonyl-CoA pathway. The activity of the key enzyme of the pathway, propionyl-CoA carboxylase (PCC), was upregulated 20-fold during growth with propio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::717ce959e8259cdf1f4e26b1ade9a553
https://doi.org/10.1128/jb.00402-15
https://doi.org/10.1128/jb.00402-15
Autor:
Birgit E. Alber, Marie Asao
Publikováno v:
Journal of Bacteriology. 195:4716-4725
The anoxygenic phototroph Rhodobacter sphaeroides uses 3-hydroxypropionate as a sole carbon source for growth. Previously, we showed that the gene (RSP_1434) known as acuI , which encodes a protein of the medium-chain dehydrogenase/reductase (MDR) su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd9c629462df46fcc8dc200b1450f755
https://doi.org/10.1128/jb.00685-13
https://doi.org/10.1128/jb.00685-13
Publikováno v:
Journal of Bacteriology. 192:1249-1258
Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24884957dd155cf1c866ebba36cd7068
https://doi.org/10.1128/jb.01267-09
https://doi.org/10.1128/jb.01267-09
Publikováno v:
Journal of Bacteriology. 191:4572-4581
A 3-hydroxypropionate/4-hydroxybutyrate cycle operates in autotrophic CO 2 fixation in various Crenarchaea , as studied in some detail in Metallosphaera sedula . This cycle and the autotrophic 3-hydroxypropionate cycle in Chloroflexus aurantiacus hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1ce3610552539f6a2c79f8a600578e5
https://doi.org/10.1128/jb.00068-09
https://doi.org/10.1128/jb.00068-09
Publikováno v:
Journal of Bacteriology. 188:6460-6468
The phototrophic bacterium Chloroflexus aurantiacus uses the 3-hydroxypropionate cycle for autotrophic CO 2 fixation. This cycle starts with acetyl-coenzyme A (CoA) and produces glyoxylate. Glyoxylate is an unconventional cell carbon precursor that n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d51a4eaa891a49c661005b14bea4b635
https://doi.org/10.1128/jb.00659-06
https://doi.org/10.1128/jb.00659-06
Publikováno v:
Molecular Microbiology. 61:297-309
Organisms, which grow on organic substrates that are metabolized via acetyl-CoA, are faced with the problem to form all cell constituents from this C(2)-unit. The problem was solved by the seminal work of Kornberg and is known as the glyoxylate cycle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64ea71e9c994cfaf05144c5493c44966
https://doi.org/10.1111/j.1365-2958.2006.05238.x
https://doi.org/10.1111/j.1365-2958.2006.05238.x
Publikováno v:
Biochemistry. 39:9222-9231
The prototype of the gamma-class of carbonic anhydrase has been characterized from the methanogenic archaeon Methanosarcina thermophila. Previously reported kinetic studies of the gamma-class carbonic anhydrase are consistent with this enzyme having
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ea8965c3549c1077e2b007a95c1407b
https://doi.org/10.1021/bi000204s
https://doi.org/10.1021/bi000204s
Autor:
James G. Ferry, Birgit E. Alber
Publikováno v:
Journal of Bacteriology. 178:3270-3274
The gene encoding carbonic anhydrase from Methanosarcina thermophila was hyperexpressed in Escherichia coli, and the heterologously produced enzyme was purified 14-fold to apparent homogeneity. The enzyme purified from E. coli has properties (specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff02ec7879fb3aee548701ab8df2c877
https://doi.org/10.1128/jb.178.11.3270-3274.1996
https://doi.org/10.1128/jb.178.11.3270-3274.1996
Publikováno v:
The EMBO Journal. 15:2323-2330
A carbonic anhydrase from the thermophilic archaeon Methanosarcina thermophila that exhibits no significant sequence similarity to known carbonic anhydrases has recently been characterized. Here we present the structure of this enzyme, which adopts a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9efc3afeecb998b0b8064a999990b886
https://doi.org/10.1002/j.1460-2075.1996.tb00588.x
https://doi.org/10.1002/j.1460-2075.1996.tb00588.x