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EC Number
Title
Organism
1.14.13.44
A crystal structure of 2-hydroxybiphenyl 3-monooxygenase with bound substrate provides insights into the enzymatic mechanism
Pseudomonas nitroreducens
1.14.13.44
Altering 2-hydroxybiphenyl 3-monooxygenase regioselectivity by protein engineering for the production of a new antioxidant
Pseudomonas nitroreducens
1.14.13.44
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases
Pseudomonas nitroreducens
1.14.13.44
Structures of the Apo and FAD-bound forms of 2-hydroxybiphenyl 3-monooxygenase (HbpA) locate activity hotspots identified by using directed evolution
Pseudomonas nitroreducens
1.14.13.44
An integrated process for the production of toxic catechols from toxic phenols based on a designer biocatalyst
Escherichia coli
1.14.13.44
An integrated process for the production of toxic catechols from toxic phenols based on a designer biocatalyst
Escherichia coli JM101
1.14.13.44
Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1
Pseudomonas nitroreducens
1.14.13.44
Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1
Pseudomonas nitroreducens HBP1
1.14.13.44
Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution
Pseudomonas nitroreducens
1.14.13.44
Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution
Pseudomonas nitroreducens HBP1
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