Zobrazeno 1 - 10
of 21
pro vyhledávání: '"O. P. Peoples"'
Publikováno v:
Journal of Bacteriology. 175:4096-4103
Two promoters required for expression of the ask-asd genes, encoding aspartokinase (AK) and aspartate-semialdehyde dehydrogenase (ASD), in Corynebacterium flavum N13, askP1 and askP2, have been identified by deletion analysis and S1 nuclease mapping.
Autor:
Christopher T. Walsh, Anthony J. Sinskey, O. P. Peoples, Simon F. Williams, M. A. J. Palmer, Satoru Masamune, R. Gamboni, E. Differding
Publikováno v:
Journal of Biological Chemistry. 266:8369-8375
Biosynthetic thiolase from Zoogloea ramigera was inactivated with a mechanism-based inactivator, 3-pentynoyl-S-pantetheine-11-pivalate (3-pentynoyl-SPP) where K1 = 1.25 mM and kinact = 0.26 min-1, 2,3-pentadienoyl-SPP obtained from nonenzymatic rearr
Autor:
Satoru Masamune, Anthony J. Sinskey, Christopher T. Walsh, O. P. Peoples, M. A. J. Palmer, Simon F. Williams
Publikováno v:
Journal of Biological Chemistry. 267:16041-16043
The proposed active-site base Cys-378 of thiolase, responsible for deprotonation of acetyl-CoA, has been converted to a less acidic residue Ser-378 by mutagenesis. Comparison of the CD spectra and dimethyl suberimidate cross-linking experiments of th
Autor:
JoAnne Stubbe, Kristi D. Snell, E. Csuhai, Satoru Masamune, O. P. Peoples, Anthony J. Sinskey, Tillman U. Gerngross
Publikováno v:
Biochemistry. 33(31)
Polyhydroxyalkanoate (PHA) synthase has been expressed in Escherichia coli by reengineering the 5'-end of the wild-type (wt) gene and subsequent transformation of this gene into protease-deficient E. coli UT5600 (ompT-). Induction with IPTG results i
Publikováno v:
The Journal of biological chemistry. 267(23)
The proposed active-site base Cys-378 of thiolase, responsible for deprotonation of acetyl-CoA, has been converted to a less acidic residue Ser-378 by mutagenesis. Comparison of the CD spectra and dimethyl suberimidate cross-linking experiments of th
Autor:
M A, Palmer, E, Differding, R, Gamboni, S F, Williams, O P, Peoples, C T, Walsh, A J, Sinskey, S, Masamune
Publikováno v:
The Journal of biological chemistry. 266(13)
Biosynthetic thiolase from Zoogloea ramigera was inactivated with a mechanism-based inactivator, 3-pentynoyl-S-pantetheine-11-pivalate (3-pentynoyl-SPP) where K1 = 1.25 mM and kinact = 0.26 min-1, 2,3-pentadienoyl-SPP obtained from nonenzymatic rearr
Autor:
Anthony J. Sinskey, O. P. Peoples
Publikováno v:
Novel Biodegradable Microbial Polymers ISBN: 9789401074582
PHB is the most common member of the polyhydroxyalkanoate family of polyester biopolymers produced intracellularly as energy reserve materials in a large number of diverse bacteria. The physical properties of these biodegradable thermoplastics have m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d097b0c9675e3a0a62df8670d6eccf32
https://doi.org/10.1007/978-94-009-2129-0_16
https://doi.org/10.1007/978-94-009-2129-0_16
Publikováno v:
Journal of Bacteriology. 170:781-789
The gene coding for cyclohexanone monooxygenase from Acinetobacter sp. strain NCIB 9871 was isolated by immunological screening methods. We located and determined the nucleotide sequence of the gene. The structural gene is 1,626 nucleotides long and
Publikováno v:
Journal of Bacteriology. 169:4518-4524
The genetics of the biosynthesis of an exocellular polysaccharide (EPS) from Zoogloea ramigera I-16-M is being investigated. Tn5 insertion mutants deficient in EPS production were isolated by screening for the absence of fluorescence on plates contai
Publikováno v:
Pure and Applied Chemistry. 61:303-312
Abstrad - The organisms Zoogloea ramigera and Alcaligenes eutrophus, like many other bacteria, produce poly-(~-3-hydroxybutyrate (PHB) from acetyl-CoA through the threeenzyme pathway involving thiolase, reductase and PHB synthase. Thiolase catalyzes