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| rdf:type
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| Description
| - A novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC_JF8) catalyzing the meta-cleavage of the hydroxylated biphenyl ring was purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8 and the gene cloned. The native and recombinant BphC enzyme was purified to homogeneity. The enzyme has a molecular mass of 125+-10 kDa and was composed of 4 identical subunits (35 kDa). BphC_JF8 has a temperature optimum of 85 C and a pH optimum of 8.5. It exhibited a half life of 30 min at 80 C and 81 min at 75 C, making it the most thermostable extradiol dioxygenase studied. ICP-MS analysis confirmed the presence of 4.0 to 4.8 manganese atoms per enzyme molecule. The ESR spectrum of BphC_JF8 exhibited g = 2.02 and g = 4.06 signals having the 6-fold hyperfine splitting characteristic of Mn(II). The enzyme can oxidize a wide range of substrates and the substrate preference was in the order 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-methylcatechol
- A novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC_JF8) catalyzing the meta-cleavage of the hydroxylated biphenyl ring was purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8 and the gene cloned. The native and recombinant BphC enzyme was purified to homogeneity. The enzyme has a molecular mass of 125+-10 kDa and was composed of 4 identical subunits (35 kDa). BphC_JF8 has a temperature optimum of 85 C and a pH optimum of 8.5. It exhibited a half life of 30 min at 80 C and 81 min at 75 C, making it the most thermostable extradiol dioxygenase studied. ICP-MS analysis confirmed the presence of 4.0 to 4.8 manganese atoms per enzyme molecule. The ESR spectrum of BphC_JF8 exhibited g = 2.02 and g = 4.06 signals having the 6-fold hyperfine splitting characteristic of Mn(II). The enzyme can oxidize a wide range of substrates and the substrate preference was in the order 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-methylcatechol (en)
- A novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC_JF8) catalyzing the meta-cleavage of the hydroxylated biphenyl ring was purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8 and the gene cloned. The native and recombinant BphC enzyme was purified to homogeneity. The enzyme has a molecular mass of 125+-10 kDa and was composed of 4 identical subunits (35 kDa). BphC_JF8 has a temperature optimum of 85 C and a pH optimum of 8.5. It exhibited a half life of 30 min at 80 C and 81 min at 75 C, making it the most thermostable extradiol dioxygenase studied. ICP-MS analysis confirmed the presence of 4.0 to 4.8 manganese atoms per enzyme molecule. The ESR spectrum of BphC_JF8 exhibited g = 2.02 and g = 4.06 signals having the 6-fold hyperfine splitting characteristic of Mn(II). The enzyme can oxidize a wide range of substrates and the substrate preference was in the order 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-methylcatechol (cs)
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| Title
| - Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8
- Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8 (en)
- Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8 (cs)
|
| skos:prefLabel
| - Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8
- Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8 (en)
- Cloning and characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB and naphthalene degrading Bacillus sp. JF8 (cs)
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| skos:notation
| - RIV/00216224:14310/03:00008775!RIV08-MSM-14310___
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/03:00008775
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - ENZYME; THERMOSTABILITY; PCB; BIODEGRADATION; CLONING (en)
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| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
| - Journal of Biological Chemistry
|
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Damborský, Jiří
- Kimbara, Kazuhide
- Hatta, Takashi
- Kiyohara, Hohzoh
- Mukerjee-Dhar, Gouri
|
| number of pages
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| http://localhost/t...ganizacniJednotka
| |
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