1.14.13.44: 2-hydroxybiphenyl 3-monooxygenase
This is an abbreviated version!
For detailed information about 2-hydroxybiphenyl 3-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.44
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1.14.13.44
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azelaica
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phenol
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fad
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2-substituted
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flavin
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2,3-dihydroxybiphenyl
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biocatalytic
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non-substrate
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laboratory-evolved
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amberlite
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fad-dependent
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entrance
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ortho-hydroxylation
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flavoprotein
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catechols
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synthesis
- 1.14.13.44
- azelaica
- phenol
- fad
-
2-substituted
- flavin
- 2,3-dihydroxybiphenyl
-
biocatalytic
-
non-substrate
-
laboratory-evolved
-
amberlite
-
fad-dependent
-
entrance
-
ortho-hydroxylation
- flavoprotein
- catechols
- synthesis
Reaction
Synonyms
2-hydroxybiphenyl 3-monooxygenase, HBP1, HbpA, oxygenase, 2-hydroxybiphenyl 3-mono-
ECTree
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General Information
General Information on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase
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physiological function
additional information
2-hydroxybiphenyl 3-monooxygenase is a flavin-containing NADH-dependent aromatic hydroxylase that oxidizes a broad range of 2-substituted phenols
physiological function
HbpA hydroxylates its substrate 2-hydroxybiphenyl to 2,3-dihydroxybiphenyl
residue Trp97 stabilizes the substrate in the active site, residue Met223 is involved in NADH entrance or binding to the active site, and residue Pro320 might facilitate FAD movement. Molecular docking study with wild-type and mutant enzymes and FAD and substrates
additional information
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA, PDB ID 4cy8) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
additional information
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sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA, PDB ID 4cy8) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases