Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
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Agarose and Its Derivatives as Supports for Enzyme ImmobilizationSpatial organization of multi-enzyme biocatalytic cascades.Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor.Heterogeneous Systems Biocatalysis: The Path to the Fabrication of Self-Sufficient Artificial Metabolic Cells.Structure-guided design of Serratia marcescens short-chain dehydrogenase/reductase for stereoselective synthesis of (R)-phenylephrine.Preserving enzymatic activity and enhancing biochemical stability of glutathione transferase by soluble additives under free and tethered conditions.
P2860
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
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2015 nî lūn-bûn
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name
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@en
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@nl
type
label
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@en
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@nl
prefLabel
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@en
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor.
@nl
P50
P1476
Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor
@en
P2093
Marzena Krzek
P304
P356
10.1016/J.ENZMICTEC.2015.09.006
P577
2015-09-30T00:00:00Z