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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND CHARACTERIZATION.
DOI=10.1074/jbc.M210240200; PubMed=12672826 [NCBI, ExPASy, EBI, Israel, Japan]
Hatta T.,
Mukerjee-Dhar G.,
Damborsky J.,
Kiyohara H.,
Kimbara K.;
"Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.";
J. Biol. Chem. 278:21483-21492(2003).
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- FUNCTION: Catalyzes the meta-cleavage of the hydroxylated biphenyl ring. The enzyme can oxidize a wide range of substrates, and the substrate preference order is 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-methylcatechol > 4-chlorocatechol.
- CATALYTIC ACTIVITY: Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O.
- COFACTOR: Binds 1 manganese ion per subunit.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=0.095 µM for 2,3-dihydroxybiphenyl (at 60 degrees Celsius and pH 7.5); | | KM=1.0 µM for 3-methylcatechol (at 60 degrees Celsius and pH 7.5); | | KM=25.0 µM for 4-chlorocatechol (at 60 degrees Celsius and pH 7.5); | | KM=103.0 µM for catechol (at 60 degrees Celsius and pH 7.5); | | KM=111.0 µM for 4-methylcatechol (at 60 degrees Celsius and pH 7.5); | | Vmax=5.7 µmol/min/mg enzyme with 2,3-dihydroxybiphenyl as substrate (at 60 degrees Celsius and pH 7.5); | | Vmax=3.4 µmol/min/mg enzyme with 3-methylcatechol as substrate (at 60 degrees Celsius and pH 7.5); | | Vmax=1.8 µmol/min/mg enzyme with catechol as substrate (at 60 degrees Celsius and pH 7.5); | | Vmax=1.3 µmol/min/mg enzyme with 4-methylcatechol as substrate (at 60 degrees Celsius and pH 7.5); | | Vmax=0.68 µmol/min/mg enzyme with 4-chlorocatechol as substrate (at 60 degrees Celsius and pH 7.5); | | pH dependence: |
Optimum pH is 7.5; | | Temperature dependence: |
Optimum temperature is 85 degrees Celsius; | |
- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 3/4.
- SUBUNIT: Homotetramer.
- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 315 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36323 Da [This is the MW of the unprocessed precursor] |
CRC64: 306CD094914E1AF4 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MTAEIAKFGH IALITPNLEK SVWFFRDIVG LEEVDRQGDT IFLRAWGDWE HHTLSLTPGN
70 80 90 100 110 120
RARVDHIAWR TKRPEDVETF AEQLKAKGTE VQWIEPGEEK GQGKAIRFRL PNGYPFEIYY
130 140 150 160 170 180
DVEKPKAPEG KKSRLKNNVY RPSYGIAPRR IDHVNVWTTN PSEIHQWLKD NMGFKMREYI
190 200 210 220 230 240
RLNNGFVAGG WMSVTPLVHD IGVMVDPKGQ PNRLHHFAYY LDNVTDILRA ADILREHDIT
250 260 270 280 290 300
IEMGGPGRHG ISQAFFLYVK DPGSGHRLEL FSGGYLIFDP DWEPIEWQEH ELQEGLIWYG
310
PEMKPGGPMD DTTEC
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Q8GR45 in FASTA format |
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