Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Acetoacetate decarboxylase activity"'
Autor:
T. William Knight, Zahra Mashhadi, Alan W. Schwabacher, Robert W. Hoppe, Hagemann Trevor, Lisa S. Mydy, Todd R. Miller, Tyler Grant Fenske, Lanlan Han, Nicholas R. Silvaggi
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 73:672-681
The Gram-negative bacterium Sphingomonas wittichii RW1 is notable for its ability to metabolize a variety of aromatic hydrocarbons. Not surprisingly, the S. wittichii genome contains a number of putative aromatic hydrocarbon-degrading gene clusters.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56740b597f918f4a11f883a175ac631e
https://doi.org/10.1107/s2053230x17015862
https://doi.org/10.1107/s2053230x17015862
Autor:
Helga Grupe, Gerhard Gottschalk
Publikováno v:
Applied and environmental microbiology. 58(12)
The pH of continuous cultures of Clostridium acetobutylicum growing at pH 5.6 was allowed to decrease to 4.3 after acid production and thereby to shift the cultures from acetate and butyrate to acetone and butanol formation. Several parameters were d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d8a0ed1126eb74a3a9b689f9a521a93
https://pubmed.ncbi.nlm.nih.gov/16348821
https://pubmed.ncbi.nlm.nih.gov/16348821
Autor:
López-Soriano Fj, Argilés Jm
Publikováno v:
Hormone and Metabolic Research. 18:446-449
21-day pregnant rats show high tissular and plasmatic acetone concentrations when submitted to a 48-hr fast. This rise is, in fact, associated with an enhanced placental and fetal acetoacetate decarboxylase activity. We propose that acetone formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50233db78d3e84a18f9e9c2381df0ef6
https://doi.org/10.1055/s-2007-1012342
https://doi.org/10.1055/s-2007-1012342
Autor:
Jiann-Shin Chen, Hugh A. George
Publikováno v:
Applied and Environmental Microbiology. 46:321-327
Factors that may initiate the metabolic transition for butanol production were investigated in batch cultures of Clostridium beijerinckii (synonym, Clostridium butylicum ) VPI 13436. Cultures maintained at pH 6.8 produced nearly as much butanol as th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3460865e678f614573f0aba86e627120
https://doi.org/10.1128/aem.46.2.321-327.1983
https://doi.org/10.1128/aem.46.2.321-327.1983
Publikováno v:
Clinica Chimica Acta. 71:173-183
In this article further information is presented about the characteristics of the mammalian enzyme acetoacetate decarboxylase (acetoacetate carboxylyase, EC 4.1.1.4). The Michaelis-Menten plot shows a sigmoidal relationship between the enzyme activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32ddb59b8079e8d97b5691cd637d6fef
https://doi.org/10.1016/0009-8981(76)90528-3
https://doi.org/10.1016/0009-8981(76)90528-3
Publikováno v:
Journal of the agricultural chemical society of Japan. 42:311-314
Acetoacetate decarboxylase activity of cell suspension of Clostridium acetobutylicum No. 314 was measured under hydrogen gas phase. When acetate buffer was used, the hydrogen uptake was observed at pH 5.0 after almost 90% of acetoacetate had been dec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6afa77101908d709e8ffed3730ff2486
https://doi.org/10.1271/nogeikagaku1924.42.6_311
https://doi.org/10.1271/nogeikagaku1924.42.6_311
Publikováno v:
Annales de l'Institut Pasteur. Microbiology. 139(6)
The activity of two enzymes involved in acetone production in Clostridium acetobutylicum, acetoacetate decarboxylase and coenzyme A transferase, was studied under acidogenic or solventogenic conditions. Acetoacetate decarboxylase activity was low und
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a82852596413229cb3f7af41985b0476
https://pubmed.ncbi.nlm.nih.gov/3252905
https://pubmed.ncbi.nlm.nih.gov/3252905
Publikováno v:
Clinica chimica acta; international journal of clinical chemistry. 39(1)
In this article evidence is presented for the existence of mammalian acetoacetate decarboxylase (acetoacetate carboxy-lyase: E.G. 4.1.1.4). From experiments with human blood serum the presence of a non-ultrafiltrable activator, accelerating the decom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cfacd6194252314bd6ec7354b593bdc
https://pubmed.ncbi.nlm.nih.gov/4624981
https://pubmed.ncbi.nlm.nih.gov/4624981