Zobrazeno 1 - 10
of 416
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
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
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.
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
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
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
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
Publikováno v:
Microbiology-Uk, 145(3), 561-568. MAIK NAUKA/INTERPERIODICA/SPRINGER
A new insertion sequence (IS2112) was identified in the genome of the 1-haloalkane-utilizing bacterium Rhodococcus rhodochrous NCIMB 13064. The insertion element is 1415 bp long, does not contain terminal inverted repeats, and is not flanked by direc