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Enzymatic Properties of Terephthalate 1,2-Dioxygenase ofComamonassp. Strain E6

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Outgoing claims: the papers this work cites, builds on, or argues with.

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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
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Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase
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Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
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Molecular and biochemical analysis of phthalate and terephthalate degradation byRhodococcussp. strain DK17
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Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1.
inferredcites →https://doi.org/10.1016/s0021-9258(19)69675-4openalex-snapshot
Purification and properties of NADH-ferredoxinTOL reductase. A component of toluene dioxygenase from Pseudomonas putida.
inferredcites →https://doi.org/10.1016/s0022-2836(02)00039-6openalex-snapshot
X-ray Crystal Structure of Benzoate 1,2-Dioxygenase Reductase from Acinetobacter sp. Strain ADP1
inferredcites →https://doi.org/10.1016/s0022-2836(83)80284-8openalex-snapshot
Studies on transformation of Escherichia coli with plasmids
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Structure-function Analysis of the Bacterial Aromatic Ring-hydroxylating Dioxygenases
inferredcites →https://doi.org/10.1016/s0378-1097(03)00124-1openalex-snapshot
Purification and gene cloning of the oxygenase component of the terephthalate 1,2-dioxygenase system fromDelftia tsuruhatensisstrain T7
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Studies on plant amylases
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2-Oxo-1,2-dihydroquinoline 8-Monooxygenase, a Two-component Enzyme System from Pseudomonas putida 86
inferredcites →https://doi.org/10.1128/aem.01270-09openalex-snapshot
Characterization of the Isophthalate Degradation Genes of Comamonas sp. Strain E6
inferredcites →https://doi.org/10.1128/aem.68.12.5882-5890.2002openalex-snapshot
Purification and Characterization of Carbazole 1,9a-Dioxygenase, a Three-Component Dioxygenase System of Pseudomonas resinovorans Strain CA10
inferredcites →https://doi.org/10.1128/aem.72.3.1825-1832.2006openalex-snapshot
Characterization of the Terephthalate Degradation Genes of Comamonas sp. Strain E6
inferredcites →https://doi.org/10.1128/jb.01322-06openalex-snapshot
Transcriptomic Analysis Reveals a Bifurcated Terephthalate Degradation Pathway in Rhodococcus sp. Strain RHA1
inferredcites →https://doi.org/10.1128/jb.155.2.505-511.1983openalex-snapshot
Naphthalene dioxygenase: purification and properties of a terminal oxygenase component
inferredcites →https://doi.org/10.1128/jb.172.1.457-464.1990openalex-snapshot
Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
inferredcites →https://doi.org/10.1128/jb.176.21.6644-6652.1994openalex-snapshot
Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component
inferredcites →https://doi.org/10.1289/ehp.95103s49openalex-snapshot
Molecular Analysis of Isophthalate and Terephthalate Degradation by Comamonas testosteroni YZW-D

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Recent advances in the biological depolymerization and upcycling of polyethylene terephthalate
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Adaptive laboratory evolution and genetic engineering improved terephthalate utilization in Pseudomonas putida KT2440
inferred← citeshttps://doi.org/10.1021/acs.jpclett.6c00584openalex-snapshot
Bidirectional Electron Transfer by a [2Fe-2S] Rieske Cluster Enables HO–Fe III ═O •– Chemistry for cis -Dihydroxylation
inferred← citeshttps://doi.org/10.1021/acssuschemeng.4c00363openalex-snapshot
One-Pot Microbial Cell Factory Strategy for the Production of Protocatechuic Acid from Polyethylene Terephthalate Waste
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Microbial synthesis of vanillin from waste poly(ethylene terephthalate)
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Microbial degradation of phthalates: biochemistry and environmental implications
inferred← citeshttps://doi.org/10.1111/j.1574-6968.2012.02521.xopenalex-snapshot
Regulation of the isophthalate catabolic operon controlled by IphR in Comamonas sp. strain E6
inferred← citeshttps://doi.org/10.1128/aem.01270-09openalex-snapshot
Characterization of the Isophthalate Degradation Genes of Comamonas sp. Strain E6
inferred← citeshttps://doi.org/10.1128/genomea.00643-15openalex-snapshot
Draft Genome Sequence of Comamonas sp. Strain E6 (NBRC 107749), a Degrader of Phthalate Isomers through the Protocatechuate 4,5-Cleavage Pathway
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Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation
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Efficient biodegradation and upcycling of polyethylene terephthalate mediated by cell-factories
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