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ATCC ohpa homologue

Putative <t>2‐hydroxyphenylacetate</t> <t>(2‐HPA)</t> degradation pathway and gene clusters involved in 2‐HPA catabolism in Cupriavidus pinatubonensis JMP134. A. C. pinatubonensis JMP134 route channelling degradation of 2‐HPA, 3‐HPA and 4‐HPA through homogentisate producing acetoacetate and fumarate (adapted from Pérez‐Pantoja et al ., ). B. Genes putatively involved in 2‐HPA/homogentisate catabolism in strain JMP134. C. Protein domain structures of self‐sufficient cytochrome P450 enzyme encoded by <t>ohpA</t> gene. The two fused domains are shown in bold. Specific functions are indicated in thin‐lines boxes. The protein residue 388 Cysteine (haem‐iron proximal ligand) is underlined. C1: Main chromosome; C2: Secondary chromosome.

Ohpa Homologue, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ohpa homologue - by Bioz Stars, 2026-11

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1) Product Images from "Identification of a self‐sufficient cytochrome P450 monooxygenase from Cupriavidus pinatubonensis JMP134 involved in 2‐hydroxyphenylacetic acid catabolism, via homogentisate pathway"

Article Title: Identification of a self‐sufficient cytochrome P450 monooxygenase from Cupriavidus pinatubonensis JMP134 involved in 2‐hydroxyphenylacetic acid catabolism, via homogentisate pathway

Journal: Microbial Biotechnology

doi: 10.1111/1751-7915.13865

Putative 2‐hydroxyphenylacetate (2‐HPA) degradation pathway and gene clusters involved in 2‐HPA catabolism in Cupriavidus pinatubonensis JMP134. A. C. pinatubonensis JMP134 route channelling degradation of 2‐HPA, 3‐HPA and 4‐HPA through homogentisate producing acetoacetate and fumarate (adapted from Pérez‐Pantoja et al ., ). B. Genes putatively involved in 2‐HPA/homogentisate catabolism in strain JMP134. C. Protein domain structures of self‐sufficient cytochrome P450 enzyme encoded by ohpA gene. The two fused domains are shown in bold. Specific functions are indicated in thin‐lines boxes. The protein residue 388 Cysteine (haem‐iron proximal ligand) is underlined. C1: Main chromosome; C2: Secondary chromosome.

Figure Legend Snippet: Putative 2‐hydroxyphenylacetate (2‐HPA) degradation pathway and gene clusters involved in 2‐HPA catabolism in Cupriavidus pinatubonensis JMP134. A. C. pinatubonensis JMP134 route channelling degradation of 2‐HPA, 3‐HPA and 4‐HPA through homogentisate producing acetoacetate and fumarate (adapted from Pérez‐Pantoja et al ., ). B. Genes putatively involved in 2‐HPA/homogentisate catabolism in strain JMP134. C. Protein domain structures of self‐sufficient cytochrome P450 enzyme encoded by ohpA gene. The two fused domains are shown in bold. Specific functions are indicated in thin‐lines boxes. The protein residue 388 Cysteine (haem‐iron proximal ligand) is underlined. C1: Main chromosome; C2: Secondary chromosome.

Techniques Used: Residue

Transcript levels of putative 2‐hydroxyphenylacetate (2‐HPA) degradation genes from Cupriavidus pinatubonensis cells exposed to different phenylacetate compounds. Real‐time PCR analysis was performed for ohpR , ohpT , ohpA and hmgA genes expression in cells grown on phenylacetate (PA), 2‐HPA, 3‐HPA, 4‐HPA or fructose (control) as a sole carbon and energy sources. Transcript levels were normalized to the average value of transcript levels in fructose treatment. Additionally, 16S rRNA levels were used as a reference gene (internal control). All experiments were performed in three biological replicates. Error bars represent SEM. Different letters indicate statistically significant differences between treatments for each gene (one‐way analysis of variance, P < 0.05; Tukey’s test, P < 0.05), specifically in this graph the statistical group including 2‐HPA treatment (a) had a significantly much higher transcript levels as compared to any other groups (b, c, bc). The transcript levels of hmgA when cells were grown on 3‐HPA or 4‐HPA are also included in this statistical group (a).

Figure Legend Snippet: Transcript levels of putative 2‐hydroxyphenylacetate (2‐HPA) degradation genes from Cupriavidus pinatubonensis cells exposed to different phenylacetate compounds. Real‐time PCR analysis was performed for ohpR , ohpT , ohpA and hmgA genes expression in cells grown on phenylacetate (PA), 2‐HPA, 3‐HPA, 4‐HPA or fructose (control) as a sole carbon and energy sources. Transcript levels were normalized to the average value of transcript levels in fructose treatment. Additionally, 16S rRNA levels were used as a reference gene (internal control). All experiments were performed in three biological replicates. Error bars represent SEM. Different letters indicate statistically significant differences between treatments for each gene (one‐way analysis of variance, P < 0.05; Tukey’s test, P < 0.05), specifically in this graph the statistical group including 2‐HPA treatment (a) had a significantly much higher transcript levels as compared to any other groups (b, c, bc). The transcript levels of hmgA when cells were grown on 3‐HPA or 4‐HPA are also included in this statistical group (a).

Techniques Used: Real-time Polymerase Chain Reaction, Expressing, Control

Growth on 2‐HPA of Cupriavidus pinatubonensis JMP134, Pseudomonas putida KT2440 and their derivatives. A. Growth of C. pinatubonensis wild type (JMP134), ohpA mutant (JMP134d ohpA ) and ohpA mutant expressing ohpA gene driven by a heterologous P BAD promoter (JMP134d ohpA pBS1‐ ohpA ), on 2‐HPA as a sole carbon and energy source, in the presence or absence of l ‐arabinose. B. Growth of P. putida KT2440 and its derivative expressing ohpA gene driven by the heterologous P BAD promoter (KT2440 pBS1‐ ohpA ), on 2‐HPA as a sole carbon and energy source, in the presence or absence of l ‐arabinose. Three biological replicates were performed for growth measurements. Error bars indicate the standard deviation.

Figure Legend Snippet: Growth on 2‐HPA of Cupriavidus pinatubonensis JMP134, Pseudomonas putida KT2440 and their derivatives. A. Growth of C. pinatubonensis wild type (JMP134), ohpA mutant (JMP134d ohpA ) and ohpA mutant expressing ohpA gene driven by a heterologous P BAD promoter (JMP134d ohpA pBS1‐ ohpA ), on 2‐HPA as a sole carbon and energy source, in the presence or absence of l ‐arabinose. B. Growth of P. putida KT2440 and its derivative expressing ohpA gene driven by the heterologous P BAD promoter (KT2440 pBS1‐ ohpA ), on 2‐HPA as a sole carbon and energy source, in the presence or absence of l ‐arabinose. Three biological replicates were performed for growth measurements. Error bars indicate the standard deviation.

Techniques Used: Mutagenesis, Expressing, Standard Deviation

Resting cell assays of Cupriavidus pinatubonensis JMP134, Pseudomonas putida KT2440 and their derivatives in presence of hydroxyphenylacetate isomers. A. Resting cells of C. pinatubonensis JMP134, and the ohpA mutant (JMP134d ohpA ) were grown on fructose 20 mM plus 2‐HPA 2.5 mM as inducer, washed and subsequently exposed to 1 mM 2‐HPA, 3‐HPA or 4‐HPA. B. Resting cells of P. putida KT2440, and the derivative expressing ohpA gene driven by the heterologous P BAD promoter (KT2440 pBS1‐ ohpA ) were grown on succinate 30 mM plus arabinose 2.5 mM as inducer, washed and subsequently exposed to 1 mM 2‐HPA, 3‐HPA or 4‐HPA. Two biological replicates were performed for growth measurements. Error bars indicate the standard deviation.

Figure Legend Snippet: Resting cell assays of Cupriavidus pinatubonensis JMP134, Pseudomonas putida KT2440 and their derivatives in presence of hydroxyphenylacetate isomers. A. Resting cells of C. pinatubonensis JMP134, and the ohpA mutant (JMP134d ohpA ) were grown on fructose 20 mM plus 2‐HPA 2.5 mM as inducer, washed and subsequently exposed to 1 mM 2‐HPA, 3‐HPA or 4‐HPA. B. Resting cells of P. putida KT2440, and the derivative expressing ohpA gene driven by the heterologous P BAD promoter (KT2440 pBS1‐ ohpA ) were grown on succinate 30 mM plus arabinose 2.5 mM as inducer, washed and subsequently exposed to 1 mM 2‐HPA, 3‐HPA or 4‐HPA. Two biological replicates were performed for growth measurements. Error bars indicate the standard deviation.

Techniques Used: Mutagenesis, Expressing, Standard Deviation

Evolutionary relationships among several OhpA homologues. Maximum likelihood topology provided by IQ‐TREE (Nguyen et al ., ) based on sequence alignments calculated using MAFFT (Katoh et al ., ) is shown with SH‐like approximate likelihood ratio support values ( n = 1000) given at each node (values > 50% are shown). Sequences indicated in bold belong to strains tested by its ability to grow in 2‐HPA as a sole carbon and energy source. Blue, α‐proteobacteria; orange, β‐proteobacteria; green, γ‐proteobacteria; yellow, Actinobacteria; red, Hydrogenophilalia class.

Figure Legend Snippet: Evolutionary relationships among several OhpA homologues. Maximum likelihood topology provided by IQ‐TREE (Nguyen et al ., ) based on sequence alignments calculated using MAFFT (Katoh et al ., ) is shown with SH‐like approximate likelihood ratio support values ( n = 1000) given at each node (values > 50% are shown). Sequences indicated in bold belong to strains tested by its ability to grow in 2‐HPA as a sole carbon and energy source. Blue, α‐proteobacteria; orange, β‐proteobacteria; green, γ‐proteobacteria; yellow, Actinobacteria; red, Hydrogenophilalia class.

Techniques Used: Sequencing

Growth on 2‐hydroxyphenylacetate (2‐HPA) of several bacterial species included in different taxonomic groups. Strains belonging to Acinetobacter , Burkholderia , Cupriavidus , Paraburkholderia , Rhodococcus and Sphingomonas genera were grown in mineral salt medium with 2.5 mM 2‐HPA as a sole carbon and energy sources. Bacterial strains that carry the ohpA gene are indicated in bold. Shading indicates optical density (OD) at 600 nm on 24, 48 and 72 h (average of two biological replicates). Lower OD at stationary phase is the result of cell clumping in some strains. A dendrogram based in GyrB sequences is shown as reference of phylogenetic relationship among close related 2‐HPA + and 2‐HPA − strains. The phylogenetic tree was constructed using IQ‐TREE (Nguyen et al ., ) based on sequence alignments calculated utilizing MAFFT (Katoh et al ., ). Acinetobacter species were supplemented with 0.25 mM tyrosine to overcome amino acid auxotrophy. The S. wittichii RW1 strain needed a previous adaptation in 2‐HPA to obtain reproducible growth.

Figure Legend Snippet: Growth on 2‐hydroxyphenylacetate (2‐HPA) of several bacterial species included in different taxonomic groups. Strains belonging to Acinetobacter , Burkholderia , Cupriavidus , Paraburkholderia , Rhodococcus and Sphingomonas genera were grown in mineral salt medium with 2.5 mM 2‐HPA as a sole carbon and energy sources. Bacterial strains that carry the ohpA gene are indicated in bold. Shading indicates optical density (OD) at 600 nm on 24, 48 and 72 h (average of two biological replicates). Lower OD at stationary phase is the result of cell clumping in some strains. A dendrogram based in GyrB sequences is shown as reference of phylogenetic relationship among close related 2‐HPA + and 2‐HPA − strains. The phylogenetic tree was constructed using IQ‐TREE (Nguyen et al ., ) based on sequence alignments calculated utilizing MAFFT (Katoh et al ., ). Acinetobacter species were supplemented with 0.25 mM tyrosine to overcome amino acid auxotrophy. The S. wittichii RW1 strain needed a previous adaptation in 2‐HPA to obtain reproducible growth.

Techniques Used: Construct, Sequencing

Figure Legend Snippet: Bacterial strains and plasmids used in this study.

Techniques Used: Plasmid Preparation, Expressing, Control

Produced:

Article Title: Methods for the treatment of disease using immunoglobulins having fc regions with altered affinities for FcgammaRactivating and FegammaRinhibiting
Article Snippet: In certain embodiments, the invention encompasses engineering an antibody (or chimeric, humanized or other engineered versions thereof), comprising the heavy chain variable domain and/or light chain variable domain of the monoclonal antibody produced by clone 2B6, 3H7, 8B5.4.3, 1D5, 2E1, 2H9, 2D11 or 1F2 having ATCC accession numbers PTA-4591, PTA-4592, PTA-7610, PTA-5958, PTA-5961, PTA-5962, PTA-5960, and PTA-5959, respectively (deposited at ATCC, 10801 University Boulevard, Manassas, Va. 02209-2011, all of which are incorporated herein by reference). .. In certain embodiments, the invention encompasses engineering an antibody (or chimeric, humanized or other engineered versions thereof), comprising the heavy chain variable domain and/or light chain variable domain of the monoclonal antibody produced by clone 2B6, 3H7, 8B5.4.3, 1D5, 2E1, 2H9, 2D11 or 1F2 having ATCC accession numbers PTA-4591, PTA-4592, PTA-7610, PTA-5958, PTA-5961, PTA-5962, PTA-5960, and PTA-5959, respectively (deposited at ATCC, 10801 University Boulevard, Manassas, Va. 02209-2011, all of which are incorporated herein by reference). ..

Article Title: Methods for the treatment of disease using immunoglobulins having fc regions with altered affinities for FcgammaRactivating and FegammaRinhibiting
Article Snippet: In specific embodiments, the invention encompasses therapeutic antibodies that immunospecifically bind FcγRIIB via their variable domains with greater affinity than FcγRIIA, e.g., antibodies derived from mouse monoclonal antibody produced by clone 2B6 or 3H7, having ATCC accession numbers PTA-4591 and PTA-4592, respectively. .. In other embodiments, the anti-FcγRIIB antibodies of the invention are derived from a mouse monoclonal antibody produced by clone 1D5, 2E1, 2H9, 2D11, or 1F2, having ATCC Accession numbers, PTA-5958, PTA-5961, PTA-5962, PTA-5960, and PTA-5959, respectively. .. Hybridomas producing antibodies 2B6 and 3H7 have been deposited with the American Type Culture Collection (10801 University Blvd., Manassas, Va. 20110-2209) on Aug. 13, 2002 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedures, and assigned accession numbers PTA-4591 (for hybridoma producing 2B6) and PTA-4592 (for hybridoma producing 3H7), respectively, and are incorporated herein by reference.

other:

Article Title: Methods for the treatment of disease using immunoglobulins having fc regions with altered affinities for FcgammaRactivating and FegammaRinhibiting
Article Snippet: In another embodiment, an anti-FcγRIIB antibody engineered according to methods of the invention binds to the same epitope as the mouse monoclonal antibody produced from clone 2B6, 3H7, or 8B5.3.4 with ATCC accession numbers PTA-4591, PTA-4592, and PTA-7610, respectively and/or competes with the mouse monoclonal antibody produced from clone 2B6, 3H7, or 8B5.3.4 with ATCC accession numbers PTA-4591, PTA-4592, and PTA-7610, respectively as determined, e.g., in an ELISA assay or other appropriate competitive immunoassay, and also binds FcγRIIB with a greater affinity than said antibody or a fragment thereof binds FcγRIIA.

Derivative Assay:

Article Title: Methods for the treatment of disease using immunoglobulins having fc regions with altered affinities for FcgammaRactivating and FegammaRinhibiting
Article Snippet: In specific embodiments, the invention encompasses therapeutic antibodies that immunospecifically bind FcγRIIB via their variable domains with greater affinity than FcγRIIA, e.g., antibodies derived from mouse monoclonal antibody produced by clone 2B6 or 3H7, having ATCC accession numbers PTA-4591 and PTA-4592, respectively. .. In other embodiments, the anti-FcγRIIB antibodies of the invention are derived from a mouse monoclonal antibody produced by clone 1D5, 2E1, 2H9, 2D11, or 1F2, having ATCC Accession numbers, PTA-5958, PTA-5961, PTA-5962, PTA-5960, and PTA-5959, respectively. .. Hybridomas producing antibodies 2B6 and 3H7 have been deposited with the American Type Culture Collection (10801 University Blvd., Manassas, Va. 20110-2209) on Aug. 13, 2002 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedures, and assigned accession numbers PTA-4591 (for hybridoma producing 2B6) and PTA-4592 (for hybridoma producing 3H7), respectively, and are incorporated herein by reference.

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