Literature DB >> 25646545

Ring-Hydroxylating Oxygenase database: a database of bacterial aromatic ring-hydroxylating oxygenases in the management of bioremediation and biocatalysis of aromatic compounds.

Joydeep Chakraborty, Tanmoy Jana, Sudipto Saha, Tapan K Dutta.   

Abstract

Bacterial Rieske-type aromatic ring-hydroxylating oxygenases (RHOs) constitute a large family of enzymes, primarily involved in bioremediation of diverse aromatic compounds in the environment. In the present study, we have designed a manually curated database, Ring-Hydroxylating Oxygenase database (RHObase), which provides comprehensive information on all biochemically characterized bacterial RHOs. It consists of ∼ 1000 entries including 196 oxygenase α-subunits, 153 oxygenase β-subunits, 92 ferredoxins and 110 reductases, distributed among 131 different bacterial strains implementing a total of 318 oxygenation reactions. For each protein, users can get detailed information about its structure and conserved domain(s) with motif signature. RHObase allows users to search a query, based on organism, oxygenase, substrate, or protein structure. In addition, this resource provides analysis tools to perform blast search against RHObase for prediction of putative substrate(s) for the query oxygenase and its phylogenetic affiliation. Furthermore, there is an integrated cheminformatics tool to search for structurally similar compound(s) in the database vis-a-vis RHO(s) capable of transforming those compound(s). Resources in the RHObase and multiple search/display options therein are intended to provide oxygenase-related requisite information to researchers, especially working in the field of environmental microbiology and biocatalysis to attain difficult chemistry of biotechnological importance.

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Year:  2014        PMID: 25646545     DOI: 10.1111/1758-2229.12182

Source DB:  PubMed          Journal:  Environ Microbiol Rep        ISSN: 1758-2229            Impact factor:   3.541


  7 in total

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4.  PPIMpred: a web server for high-throughput screening of small molecules targeting protein-protein interaction.

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Authors:  Marianela Macchi; Sabrina Festa; Esteban Nieto; José M Irazoqui; Nelson E Vega-Vela; Howard Junca; María P Valacco; Ariel F Amadio; Irma S Morelli; Bibiana M Coppotelli
Journal:  Biotechnol Rep (Amst)       Date:  2021-01-06

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Authors:  Sabrina Festa; Bibiana Marina Coppotelli; Laura Madueño; Claudia Lorena Loviso; Marianela Macchi; Ricardo Martin Neme Tauil; María Pía Valacco; Irma Susana Morelli
Journal:  PLoS One       Date:  2017-09-08       Impact factor: 3.240

  7 in total

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