Zobrazeno 1 - 10
of 423
pro vyhledávání: '"Janssen DB"'
Autor:
Prokop, Z, Monincova, M, Chaloupkova, R, Klvana, M, Nagata, Y, Janssen, DB, Damborsky, J, Klvaňa, Martin
Publikováno v:
The Journal of Biological Chemistry, 278(46), 45094-45100. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Haloalkane dehalogenases are bacterial enzymes capable of carbon-halogen bond cleavage in halogenated compounds. To obtain insights into the mechanism of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), we studied the steady-st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::813ab0666ad143e78aae2e130eafe3cd
https://doi.org/10.1074/jbc.m307056200
https://doi.org/10.1074/jbc.m307056200
Autor:
Kamerbeek, NM, Olsthoorn, AJJ, Fraaije, MW, Janssen, DB, Kamerbeek, Nanne M., Olsthoorn, Arjen J.J.
Publikováno v:
Applied and environmental microbiology, 69(1), 419-426. AMER SOC MICROBIOLOGY
The 4-hydroxyacetophenone monooxygenase (HAPMO) from Pseudomonas fluorescens ACB catalyzes NADPH- and oxygen-dependent Baeyer-Villiger oxidation of 4-hydroxyacetophenone to the corresponding acetate ester. Using the purified enzyme from recombinant E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b3e9e91fa922ce884e7c5f1e787730
https://doi.org/10.1128/aem.69.1.419-426.2003
https://doi.org/10.1128/aem.69.1.419-426.2003
Publikováno v:
Applied and environmental microbiology, 67(8), 3406-3412. AMER SOC MICROBIOLOGY
Most aerobic biodegradation pathways for hydrocarbons involve iron-containing oxygenases. In iron-limited environments, such as the rhizosphere, this may influence the rate of degradation of hydrocarbon pollutants. We investigated the effects of iron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad1023a546eb90331c094f3a4d3a812b
https://doi.org/10.1128/aem.67.8.3406-3412.2001
https://doi.org/10.1128/aem.67.8.3406-3412.2001
Publikováno v:
Journal of Contaminant Hydrology, 44(2), 119-140
The facilitated transport of a mixture of three polycyclic aromatic hydrocarbons (PAH) (naphthalene. fluorene, and phenanthrene) by a rhamnolipid biosurfactant was determined with silica. octadecyl-coated silica, and humic acid-coated silica columns.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1c550a4c513a1bf6e13b888e33a4441
https://doi.org/10.1016/s0169-7722(00)00097-8
https://doi.org/10.1016/s0169-7722(00)00097-8
Autor:
Poelarends, GJ, Bosma, T, Kulakov, LA, Larkin, MJ, Marchesi, [No Value], Weightman, AJ, Janssen, DB, Kulakov, Leonid A., Larkin, Michael J., Marchesi, Julian R., Weightman, Andrew J.
Publikováno v:
Journal of Bacteriology, 182(10), 2725-2731. AMER SOC MICROBIOLOGY
The sequences of the 16S rRNA and haloalkane dehalogenase ( dhaA ) genes of five gram-positive haloalkane-utilizing bacteria isolated from contaminated sites in Europe, Japan, and the United States and of the archetypal haloalkane-degrading bacterium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ef42690c16eee5c976a20c95920164c
https://doi.org/10.1128/jb.182.10.2725-2731.2000
https://doi.org/10.1128/jb.182.10.2725-2731.2000
Publikováno v:
The Journal of Biological Chemistry, 271(25), 14747-14753. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Haloalkane dehalogenase converts halogenated alkanes to their corresponding alcohols, The active site is buried inside the protein and lined with hydrophobic residues, The reaction proceeds via a covalent substrate-enzyme complex, This paper describe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0b4943e3ea7502a75a55d69fa075e59
https://doi.org/10.1074/jbc.271.25.14747
https://doi.org/10.1074/jbc.271.25.14747
Publikováno v:
Biochemistry, 35(18), 5624-5632. AMER CHEMICAL SOC
Haloalkane dehalogenase converts haloalkanes to their corresponding alcohols and halides, The reaction mechanism involves the formation of a covalent alkyl-enzyme complex which is hydrolyzed by water. The active site is a hydrophobic cavity buried be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::253eb58e4e2dfb5655bd7403950e442e
https://hdl.handle.net/11370/4120c42d-0007-4b7f-ad0f-114792ccf172
https://hdl.handle.net/11370/4120c42d-0007-4b7f-ad0f-114792ccf172
Publikováno v:
European Journal of Biochemistry, 269(8), 2093-2100. Blackwell Publishing Ltd
Penicillin acylase of Escherichia colt catalyses the hydrolysis and synthesis of beta-lactam antibiotics. To study the role of hydrophobic residues in these reactions, we have mutated three active-site phenylalanines. Mutation of alphaF146, betaF24 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::86fd30ec27460d369c865c41979eb46b
https://research.rug.nl/en/publications/f9e5c976-dacd-424b-8f21-697fef95e41a
https://research.rug.nl/en/publications/f9e5c976-dacd-424b-8f21-697fef95e41a
Autor:
Fraaije, MW, Kamerbeek, NM, van Berkel, WJH, Janssen, DB, Kamerbeek, Nanne M., Berkel, Willem J.H. van
Publikováno v:
FEBS Letters, 518, 43-47
FEBS Letters, 518(1-3):PII S0014-5793(02)02623-6, 43-47. Wiley
FEBS Letters 518 (2002)
FEBS Letters, 518(1-3):PII S0014-5793(02)02623-6, 43-47. Wiley
FEBS Letters 518 (2002)
Baeyer-Villiger monooxygenases (BVMOs) form a distinct class of flavoproteins that catalyze the insertion of an oxygen atom in a C-C bond using dioxygen and NAD(P)H. Using newly characterized BVMO sequences, we have uncovered a BVMO-identifying seque
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8b363efe92f048aa2c9bee9b40d687c
https://research.wur.nl/en/publications/identification-of-a-baeyer-villiger-monooxygenase-sequence-motif
https://research.wur.nl/en/publications/identification-of-a-baeyer-villiger-monooxygenase-sequence-motif
Autor:
Alkema, WBL, Hensgens, CMH, Kroezinga, EH, de Vries, E, Floris, R, van der Laan, JM, Dijkstra, BW, Janssen, DB
Publikováno v:
Protein Engineering, 13(12), 857-863
The binding of penicillin to penicillin acylase was studied by X-ray crystallography, The structure of the enzyme-substrate complex was determined after soaking crystals of an inactive beta N241A penicillin acylase mutant with penicillin G, Binding o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::96907ba14d7803d0ce2cd223fc84fff5
https://research.rug.nl/en/publications/f7f09579-ff46-467e-8db7-4cf7bb90d17c
https://research.rug.nl/en/publications/f7f09579-ff46-467e-8db7-4cf7bb90d17c