OxDBase: a database of oxygenases involved in biodegradation.

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OxDBase: a database of oxygenases involved in biodegradation. is …
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scholarly articleQ13442814

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P6179Dimensions Publication ID1030313876
P356DOI10.1186/1756-0500-2-67
P932PMC publication ID2683861
P698PubMed publication ID19405962
P5875ResearchGate publication ID24393012

P50authorManish KumarQ56947004
G. P. S. RaghavaQ58210866
Pankaj K AroraQ83752231
P2093author name stringRakesh K Jain
Archana Chauhan
P2860cites workBiodegradation of aromatic compounds by Escherichia coliQ28208239
Aromatic hydrocarbon dioxygenases in environmental biotechnologyQ33941468
Practical issues in the application of oxygenasesQ35101084
Evolutionary relationships among extradiol dioxygenasesQ35614251
Molecular mechanisms of genetic adaptation to xenobiotic compoundsQ35655423
Bacterial degradation of aromatic pollutants: a paradigm of metabolic versatilityQ35922212
The ins and outs of ring-cleaving dioxygenases.Q36539821
Isolation of extradiol dioxygenase genes that are phylogenetically distant from other meta-cleavage dioxygenase genesQ36852955
Roles of the divergent branches of the meta-cleavage pathway in the degradation of benzoate and substituted benzoatesQ39955682
Designing microorganisms for the treatment of toxic wastesQ40572977
l-3,4-Dihydroxyphenyl alanine-extradiol cleavage is followed by intramolecular cyclization in lincomycin biosynthesis.Q45049948
Bacterial aromatic ring-cleavage enzymes are classified into two different gene families.Q48287182
P921main subjectbiodegradationQ696715
databaseQ8513
P304page(s)67
P577publication date2009-04-30
P1433published inBMC Research NotesQ15762797
P1476titleOxDBase: a database of oxygenases involved in biodegradation
P478volume2