Výsledky vyhledávání - "Birgit E. Alber"

Transcriptional Regulation by the Short-Chain Fatty Acyl Coenzyme A Regulator (ScfR) PccR Controls Propionyl Coenzyme A Assimilation by Rhodobacter sphaeroides

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

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Acrylyl-Coenzyme A Reductase, an Enzyme Involved in the Assimilation of 3-Hydroxypropionate by Rhodobacter sphaeroides

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

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https://doi.org/10.1128/jb.00685-13

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The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3 S )-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3 S )- Malyl-CoA Thioesterase

Autor: Georg Fuchs, Birgit E. Alber, Tobias J. Erb, Lena Frerichs-Revermann

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

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3-Hydroxypropionyl-Coenzyme A Dehydratase and Acryloyl-Coenzyme A Reductase, Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in the Sulfolobales

Autor: Johannes W. Kung, Robin Teufel, Birgit E. Alber, Georg Fuchs, Daniel Kockelkorn

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

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https://doi.org/10.1128/jb.00068-09

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Properties of Succinyl-Coenzyme A: d -Citramalate Coenzyme A Transferase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of Chloroflexus aurantiacus

Autor: Silke Friedmann, Georg Fuchs, Birgit E. Alber

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

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https://doi.org/10.1128/jb.00659-06

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Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides

Autor: Christa Ebenau-Jehle, Georg Fuchs, Birgit E. Alber, Regina Spanheimer

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

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https://doi.org/10.1111/j.1365-2958.2006.05238.x

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A Closer Look at the Active Site of γ-Class Carbonic Anhydrases: High-Resolution Crystallographic Studies of the Carbonic Anhydrase from Methanosarcina thermophila

Autor: Douglas C. Rees, Caroline Kisker, Birgit E. Alber, James G. Ferry, Tina M. Iverson

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

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Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila

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

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https://doi.org/10.1128/jb.178.11.3270-3274.1996

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