about
Flavin dependent monooxygenasesSphingopyxis fribergensis sp. nov., a soil bacterium with the ability to degrade styrene and phenylacetic acid.Functional characterization and stability improvement of a 'thermophilic-like' ene-reductase from Rhodococcus opacus 1CPStyrene oxide isomerase of Rhodococcus opacus 1CP, a highly stable and considerably active enzyme.FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase.Production of a recombinant membrane protein in an Escherichia coli strain for the whole cell biosynthesis of phenylacetic acids.Co-metabolic formation of substituted phenylacetic acids by styrene-degrading bacteria.Identification of a novel self-sufficient styrene monooxygenase from Rhodococcus opacus 1CP.StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase systemCatalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding.One-component styrene monooxygenases: an evolutionary view on a rare class of flavoproteins.A thermophilic-like ene-reductase originating from an acidophilic iron oxidizer.Trehalose phosphate synthases OtsA1 and OtsA2 of Rhodococcus opacus 1CP.N-terminus determines activity and specificity of styrene monooxygenase reductases.Styrene oxide isomerase of Sphingopyxis sp. Kp5.2.Engineering Styrene Monooxygenase for Biocatalysis: Reductase-Epoxidase Fusion Proteins.Changing the electron donor improves azoreductase dye degrading activity at neutral pH.Characterization of Aldehyde Dehydrogenases Applying an Enzyme Assay with In Situ Formation of Phenylacetaldehydes.Effects of citric acid and the siderophore desferrioxamine B (DFO-B) on the mobility of germanium and rare earth elements in soil and uptake in Phalaris arundinacea.A mechanistic study on SMOB-ADP1: an NADH:flavin oxidoreductase of the two-component styrene monooxygenase of Acinetobacter baylyi ADP1.Immobilization of an integral membrane protein for biotechnological phenylacetaldehyde production.Detection of arsenic-binding siderophores in arsenic-tolerating Actinobacteria by a modified CAS assay.VpStyA1/VpStyA2B of Variovorax paradoxus EPS: An Aryl Alkyl Sulfoxidase Rather than a Styrene Epoxidizing Monooxygenase.On the Enigma of Glutathione-Dependent Styrene Degradation in Gordonia rubripertincta CWB2.Gene redundancy of two-component (chloro)phenol hydroxylases in Rhodococcus opacus 1CP.A Review: The Styrene Metabolizing Cascade of Side-Chain Oxygenation as Biotechnological Basis to Gain Various Valuable Compounds.Analysis of desferrioxamine-like siderophores and their capability to selectively bind metals and metalloids: development of a robust analytical RP-HPLC methodCatalytic Performance of a Class III Old Yellow Enzyme and Its Cysteine VariantsBiodegradation of High Concentrations of Aliphatic Hydrocarbons in Soil from a Petroleum Refinery: Implications for Applicability of New Actinobacterial StrainsIdentification and characterization of a FAD-dependent putrescine N-hydroxylase (GorA) from Gordonia rubripertincta CWB2Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological OpportunitiesPyridine Nucleotide Coenzyme Specificity of -Hydroxybenzoate Hydroxylase and Related Flavoprotein MonooxygenasesEditorial: , a Source of Biocatalytic ToolsOptimization of a genome-walking method to suit GC-rich template DNA from biotechnological relevant ActinobacteriaDraft genome sequence of Kocuria indica DP-K7, a methyl red degrading actinobacteriumAsymmetric Reduction of (R)-Carvone through a Thermostable and Organic-Solvent-Tolerant Ene-ReductaseChemoenzymatic Cascade Synthesis of Optically Pure Alkanoic Acids by Using Engineered Arylmalonate Decarboxylase VariantsTwo Homologous Enzymes of the GalU Family in Rhodococcus opacus 1CP-RoGalU1 and RoGalU2Indigoid dyes by group E monooxygenases: mechanism and biocatalysisMetal binding ability of microbial natural metal chelators and potential applications
P50
Q28304493-3C1FD14A-E891-493C-A3E8-036BE4703F14Q30964781-602D0015-7B05-4910-97E6-52FC59D53427Q41548132-600CD152-48C0-4A48-8185-EE198D165047Q42064807-EC4774FB-7819-4704-B648-473C80B4B98AQ42082251-E574B904-DCBE-4963-BE62-B2F8E94DE5A0Q42114265-35AF98BF-6AD2-4FD4-8DF8-E45C020EE266Q42154276-1413AD4F-78A2-4E21-88EB-2A80B054D222Q42232506-A3269297-22E3-457E-AC7B-D694BDA9EF93Q42421275-B7D70452-B3D3-4BFE-A885-9F1F4E863250Q42573539-5F49D6F8-830C-4117-B0B5-01F114F03CE3Q42645359-D619F772-958F-459A-A5B4-4E8AA606AB0EQ43028349-6C00A609-A399-48A8-94C9-A04F6AD30C08Q44476438-2BFD2617-A32A-48F2-877B-F12858B77E44Q47828550-8A893A3C-4309-4022-9303-EBB7B86073FBQ47983798-298C3519-BB1C-4225-8F77-BB01F1107447Q48235032-86FE0E18-C0B4-4EA9-99C0-65816309D155Q50213706-C6133369-60AF-455F-B726-2E4F82855601Q50965546-47D067A0-5B2C-4EFA-9EE2-4CB0BA735086Q51232281-7734F706-1980-49C0-B1ED-2EFE2C494408Q51419610-C6627DCF-7FD5-4B22-9415-0034DFA3B510Q51472863-366A5644-9051-4CF0-8B80-58B490861990Q52604317-084353CE-A42B-4EBE-87BD-CF8F58CECD84Q52609634-7DF5DB35-20BD-4C97-8559-8F7A9D4EBFFDQ52687775-5B1CBA60-9FD6-40E1-A891-376A9B2BF9A2Q52873382-2E8DEB65-7120-450E-A5EB-0E8355328E45Q53730834-BE06A342-8614-440F-9169-1B673EF72E84Q57168549-E8F951AD-5388-4FD0-B16B-C5B43E84D005Q58122594-DB6593DD-4B09-479C-9743-65F111A5A4E1Q58221464-D5D4106E-CC10-47D6-B462-3DFCA55DCE9DQ58221482-43824EF5-74FD-4741-8A69-E94F1910AE6AQ58802616-3FEDDAAD-45F9-4BFB-9F98-0B26715EF353Q60949729-ADC09181-826A-4C86-9D55-08B92D93E866Q64108299-9BF04E03-F7BA-43CB-AEFE-63AA2DDBE5E7Q84968771-40C2B919-0E0C-4EA0-AF22-9CE05BAE3A40Q90747560-4E02566A-2441-437D-89A3-A0075A1AB1B3Q91137708-F3BCE71F-28E7-4D71-872E-B25A0E6F22F5Q91289562-AF25F239-371A-4871-ABD5-C0FC7FDB7C9BQ91377913-3FBEB0A4-BD58-49EC-AAE9-AA4070C78D3CQ92195461-4F3D4259-3D2B-43F2-949A-3116F939C6CDQ95284081-AED5DB5B-DC5E-4A24-88A9-97D15377A5AE
P50
description
hulumtues
@sq
microbiologist in Germany
@en
microbioloog in Duitsland
@nl
ricercatore
@it
հետազոտող
@hy
name
Dirk Tischler
@ast
Dirk Tischler
@en
Dirk Tischler
@es
Dirk Tischler
@nl
Dirk Tischler
@sl
type
label
Dirk Tischler
@ast
Dirk Tischler
@en
Dirk Tischler
@es
Dirk Tischler
@nl
Dirk Tischler
@sl
prefLabel
Dirk Tischler
@ast
Dirk Tischler
@en
Dirk Tischler
@es
Dirk Tischler
@nl
Dirk Tischler
@sl
P214
P1053
H-9431-2013
P106
P1153
29167596600
P19
P1960
vL0vQLQAAAAJ
P2038
Dirk_Tischler
P21
P213
0000 0004 0356 5349
P214
P2798
P31
P3829
P3835
dirk-tischler2
P496
0000-0002-6288-2403
P569
1982-01-01T00:00:00Z
P734
P735
P7859
viaf-300238124