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Journal Abstract Search
321 related items for PubMed ID: 16952935
1. Properties of succinyl-coenzyme A:D-citramalate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. Friedmann S, Alber BE, Fuchs G. J Bacteriol; 2006 Sep; 188(18):6460-8. PubMed ID: 16952935 [Abstract] [Full Text] [Related]
2. Properties of succinyl-coenzyme A:L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. Friedmann S, Steindorf A, Alber BE, Fuchs G. J Bacteriol; 2006 Apr; 188(7):2646-55. PubMed ID: 16547052 [Abstract] [Full Text] [Related]
3. Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. Friedmann S, Alber BE, Fuchs G. J Bacteriol; 2007 Apr; 189(7):2906-14. PubMed ID: 17259315 [Abstract] [Full Text] [Related]
6. Assaying for the 3-hydroxypropionate cycle of carbon fixation. Hügler M, Fuchs G. Methods Enzymol; 2005 Apr; 397():212-21. PubMed ID: 16260293 [Abstract] [Full Text] [Related]
7. L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation. Herter S, Busch A, Fuchs G. J Bacteriol; 2002 Nov; 184(21):5999-6006. PubMed ID: 12374834 [Abstract] [Full Text] [Related]
9. Presence of acetyl coenzyme A (CoA) carboxylase and propionyl-CoA carboxylase in autotrophic Crenarchaeota and indication for operation of a 3-hydroxypropionate cycle in autotrophic carbon fixation. Menendez C, Bauer Z, Huber H, Gad'on N, Stetter KO, Fuchs G. J Bacteriol; 1999 Feb; 181(4):1088-98. PubMed ID: 9973333 [Abstract] [Full Text] [Related]
10. Expression of the sub-pathways of the Chloroflexus aurantiacus 3-hydroxypropionate carbon fixation bicycle in E. coli: Toward horizontal transfer of autotrophic growth. Mattozzi Md, Ziesack M, Voges MJ, Silver PA, Way JC. Metab Eng; 2013 Mar; 16():130-9. PubMed ID: 23376595 [Abstract] [Full Text] [Related]
12. Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon metabolic pathways in bacteria. Zarzycki J, Schlichting A, Strychalsky N, Müller M, Alber BE, Fuchs G. J Bacteriol; 2008 Feb; 190(4):1366-74. PubMed ID: 18065535 [Abstract] [Full Text] [Related]
13. Chloroflexus aurantiacus acetyl-CoA carboxylase evolves fused biotin carboxylase and biotin carboxyl carrier protein to complete carboxylation activity. Shen J, Wu W, Wang K, Wu J, Liu B, Li C, Gong Z, Hong X, Fang H, Zhang X, Xu X. mBio; 2024 May 08; 15(5):e0341423. PubMed ID: 38572988 [Abstract] [Full Text] [Related]
14. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. Teufel R, Kung JW, Kockelkorn D, Alber BE, Fuchs G. J Bacteriol; 2009 Jul 08; 191(14):4572-81. PubMed ID: 19429610 [Abstract] [Full Text] [Related]
15. Rhodobacter sphaeroides uses a reductive route via propionyl coenzyme A to assimilate 3-hydroxypropionate. Schneider K, Asao M, Carter MS, Alber BE. J Bacteriol; 2012 Jan 08; 194(2):225-32. PubMed ID: 22056933 [Abstract] [Full Text] [Related]
16. [The mechanism of acetate assimilation in purple nonsulfur bacteria lacking the glyoxylate pathway: enzymes of the citramalate cycle in Rhodobacter sphaeroides]. Filatova LV, Berg IA, Krasil'nikova EN, Ivanovskiĭ RN. Mikrobiologiia; 2005 Jan 08; 74(3):319-28. PubMed ID: 16119844 [Abstract] [Full Text] [Related]
17. Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales. Kockelkorn D, Fuchs G. J Bacteriol; 2009 Oct 08; 191(20):6352-62. PubMed ID: 19684143 [Abstract] [Full Text] [Related]
19. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO(2) fixation. Hügler M, Menendez C, Schägger H, Fuchs G. J Bacteriol; 2002 May 08; 184(9):2404-10. PubMed ID: 11948153 [Abstract] [Full Text] [Related]