Relevant bibliographies by topics / Meta-fission pathway

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Academic literature on the topic 'Meta-fission pathway'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Meta-fission pathway"

1

Koh, S., M. V. McCullar, and D. D. Focht. "Biodegradation of 2,4-Dichlorophenol through a Distal meta-Fission Pathway." Applied and environmental microbiology 63, no. 5 (1997): 2054–57. http://dx.doi.org/10.1128/aem.63.5.2054-2057.1997.

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Hernáez, M. J., E. Andújar, J. L. Ríos, S. R. Kaschabek, W. Reineke, and E. Santero. "Identification of a Serine Hydrolase Which Cleaves the Alicyclic Ring of Tetralin." Journal of Bacteriology 182, no. 19 (2000): 5448–53. http://dx.doi.org/10.1128/jb.182.19.5448-5453.2000.

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ABSTRACT A gene designated thnD, which is required for biodegradation of the organic solvent tetralin by Sphingomonas macrogoltabidus strain TFA, has been identified. Sequence comparison analysis indicated that thnD codes for a carbon-carbon bond serine hydrolase showing highest similarity to hydrolases involved in biodegradation of biphenyl. An insertion mutant defective in ThnD accumulates the ring fission product which results from the extradiol cleavage of the aromatic ring of dihydroxytetralin. The gene product has been purified and characterized. ThnD is an octameric thermostable enzyme
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3

OMORI, Toshio, Hiroshi ISHIGOOKA, and Yasuji MINODA. "A new metabolic pathway for meta ring-fission compounds of biphenyl." Agricultural and Biological Chemistry 52, no. 2 (1988): 503–9. http://dx.doi.org/10.1271/bbb1961.52.503.

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4

Higson, F. K., and D. D. Focht. "Utilization of 3-chloro-2-methylbenzoic acid by Pseudomonas cepacia MB2 through the meta fission pathway." Applied and Environmental Microbiology 58, no. 8 (1992): 2501–4. http://dx.doi.org/10.1128/aem.58.8.2501-2504.1992.

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5

Bowden, Keith, and Emma J. Burgess. "Reactions of Carbonyl Compounds in Basic Solutions. Part 34. The Mechanism of the Base-Catalysed Ring Fission of 2,3-Diphenylcycloprop-2-en-1-one." Collection of Czechoslovak Chemical Communications 64, no. 10 (1999): 1594–600. http://dx.doi.org/10.1135/cccc19991594.

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The rate coefficients for the base-catalysed ring fission of a series of 2-phenyl-3-(2-, 3- or 4-substituted phenyl)cycloprop-2-en-1-ones to give the corresponding (E)-2,3-diphenylacrylic acids have been determined in water at 30.0 °C, as well as for the unsubstituted compound at 40.0, 50.0 and 60.0 °C. The effects of meta- and para-substituents on the rates have been correlated using the Hammett equation to give a reaction constant, ρ, equal to ca 1.2 at 30 °C. For the unsubstituted compound, the activation parameters have been calculated and the kinetic solvent isotope effect has been studie
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Hay, Anthony G., and Dennis D. Focht. "Cometabolism of 1,1-Dichloro-2,2-Bis(4-Chlorophenyl)Ethylene by Pseudomonas acidovorans M3GY Grown on Biphenyl." Applied and Environmental Microbiology 64, no. 6 (1998): 2141–46. http://dx.doi.org/10.1128/aem.64.6.2141-2146.1998.

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ABSTRACT 1,1-Dichloro-2,2-bis(4-chlorophenyl)ethylene (DDE), a toxic breakdown product of 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane (DDT), has traditionally been viewed as a dead-end metabolite: there are no published reports detailing enzymatic ring fission of DDE by bacteria in either soil or pure culture. In this study, we investigated the ability of Pseudomonas acidovorans M3GY to transform DDE and its unchlorinated analog, 1,1-diphenylethylene (DPE). While strain M3GY could grow on DPE, cells grown on DPE as a sole carbon source could not degrade DDE. Cells grown on biphenyl, however,
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Heesche-Wagner, Kerstin, Thomas Schwarz, and Michael Kaufmann. "Phenol degradation by an enterobacterium: aKlebsiellastrain carries a TOL-like plasmid and a gene encoding a novel phenol hydroxylase." Canadian Journal of Microbiology 45, no. 2 (1999): 162–71. http://dx.doi.org/10.1139/w98-218.

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Although phenol catabolism is described for many different microorganisms, there is no example for such a pathway in an enterobacterial strain. Here we characterize a Klebsiella oxytoca strain that grows on phenol as the only source of carbon and energy. As the key enzyme of phenol degradation, phenol hydroxylase was purified to apparent homogeneity. Compared with other phenol hydroxylases, the Klebsiella enzyme differs with respect to several properties: (i) SDS-PAGE and gel-filtration analysis of the purified protein revealed that the enzyme is a monomer with a molecular mass of 156 kDa; (ii
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8

Peng, Xue, Takashi Egashira, Kaoru Hanashiro, et al. "Cloning of a Sphingomonas paucimobilis SYK-6 Gene Encoding a Novel Oxygenase That Cleaves Lignin-Related Biphenyl and Characterization of the Enzyme." Applied and Environmental Microbiology 64, no. 7 (1998): 2520–27. http://dx.doi.org/10.1128/aem.64.7.2520-2527.1998.

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ABSTRACT Sphingomonas paucimobilis SYK-6 transforms 2,2′-dihydroxy-3,3′-dimethoxy-5,5′-dicarboxybiphenyl (DDVA), a lignin-related biphenyl compound, to 5-carboxyvanillic acid via 2,2′,3-trihydroxy-3′-methoxy-5,5′-dicarboxybiphenyl (OH-DDVA) as an intermediate (15). The ring fission of OH-DDVA is an essential step in the DDVA degradative pathway. A 15-kbEcoRI fragment isolated from the cosmid library complemented the growth deficiency of a mutant on OH-DDVA. Subcloning and deletion analysis showed that a 1.4-kb DNA fragment included the gene responsible for the ring fission of OH-DDVA. An open
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9

Díaz, Eduardo, Abel Ferrández, and José L. García. "Characterization of the hca Cluster Encoding the Dioxygenolytic Pathway for Initial Catabolism of 3-Phenylpropionic Acid in Escherichia coliK-12." Journal of Bacteriology 180, no. 11 (1998): 2915–23. http://dx.doi.org/10.1128/jb.180.11.2915-2923.1998.

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ABSTRACT We have identified, cloned, and sequenced the hcacluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid (PP) in Escherichia coli K-12. This cluster maps at min 57.5 of the chromosome and is composed of five catabolic genes arranged as a putative operon (hcaA1A2CBD) and two additional genes transcribed in the opposite direction that encode a potential permease (hcaT) and a regulator (hcaR). Sequence comparisons revealed that whilehcaA1A2CD genes encode the four subunits of the 3-phenylpropionate dioxygenase, the hcaB gene codes for the correspondin
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10

Bergeron, Janique, Darakhshan Ahmad, Diane Barriault, Angèle Larose, Michel Sylvestre, and Justin Powlowski. "Identification and mapping of the gene translation products involved in the first steps of the Comamonas testosteroni B-356 biphenyl/chlorobiphenyl biodegradation pathway." Canadian Journal of Microbiology 40, no. 9 (1994): 743–53. http://dx.doi.org/10.1139/m94-118.

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In this study, we have mapped Comamonas testosteroni B-356 genes encoding enzymes for the conversion of biphenyl and 4-chlorobiphenyl into the corresponding meta-cleavage compounds onto a 6.3-kb DNA fragment, and we have determined the subunit composition of the enzymes involved in this pathway. The various proteins encoded by this 6.3-kb DNA fragment and by subclones derived from it were overexpressed and selectively labelled using the T7 polymerase promoter system in Escherichia coli. They were then analyzed using SDS-PAGE, which allowed the encoding locus of each polypeptide to be mapped. D
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Dissertations / Theses on the topic "Meta-fission pathway"

1

Taylor, Stephanie Michelle 1985. "Biosynthesis of coenzyme M and the catabolism of halogenated aromatic compounds." Thesis, 2012. http://hdl.handle.net/2152/28462.

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Methanogens, members of the domain Archaea, are unique in their ability to reduce carbon substrates to methane. Coenzyme M (CoM) is required in all methanogenic pathways. The biosynthesis of this coenzyme has been well studied in Class I Methanogens, but in Class II Methanogens, such as Methanosarcina acetivorans, little is known. The first step in the biosynthetic pathway might be catalyzed by cysteate synthase (CS), which converts phosphoserine to cysteate by the addition of sulfite. The 46 kDa enzyme was successfully purified from inclusion bodies and characterized. The identity of the p
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2

Miller, Scott Garrett. "Mutagenic analysis of the decarboxylases and hydratases in parallel meta-fission pathways." 2008. http://hdl.handle.net/2152/17940.

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The catechol meta-fission pathway, a degradation pathway for simple aromatic compounds, is rich in enzyme chemistry and replete with structural and evolutionary diversity. Vinyl pyruvate hydratase (VPH) and MhpD catalyze the same reaction in this pathway, but in different bacterial species. These metal ion-dependent enzymes reportedly catalyze a 1,5-keto-enol tautomerization reaction followed by a Michael addition of water. MhpD, and most likely VPH, are members of the fumarylacetoacetate hydrolase (FAH) superfamily. The crystal structure of MhpD and the sequence of VPH identified four potenti
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