pseudomonas putida trevisan migula mnb1 (ATCC)


Structured Review
![Comparison of the theoretical structure of CumA from <t>Pseudomonas</t> <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0277/pmc10890277/pmc10890277__life-14-00171-g001.jpg)
Pseudomonas Putida Trevisan Migula Mnb1, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pseudomonas putida trevisan migula mnb1/product/ATCC
Average 94 stars, based on 1 article reviews
Images
1) Product Images from "Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation"
Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation
Journal: Life
doi: 10.3390/life14020171
![Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( ... Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0277/pmc10890277/pmc10890277__life-14-00171-g001.jpg)
Figure Legend Snippet: Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
Techniques Used: Comparison, Sequencing