scholarly journals Fungal Dirigent Protein Controls the Stereoselectivity of Multicopper Oxidase-Catalyzed Phenol Coupling in Viriditoxin Biosynthesis

2019 ◽  
Author(s):  
Jinyu Hu ◽  
Hang Li ◽  
Yit-Heng Chooi
Keyword(s):  
Multicopper Oxidase ◽  
Dirigent Protein

scholarly journals Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Erika Berenice Martínez-Ruiz ◽  
Myriel Cooper ◽  
Jimena Barrero-Canosa ◽  
Mindia A. S. Haryono ◽  
Irina Bessarab ◽  
...  
Keyword(s):  
Calvin Cycle ◽  
Multicopper Oxidase ◽  
Genomic Islands ◽  
Biotechnological Applications ◽  
High Similarity ◽  
Multicopper Oxidases ◽  
Metabolic Potential ◽  
Natural Habitats ◽  
Manganese Oxidation ◽  
Wide Range

Abstract Background Cylindrospermopsin is a highly persistent cyanobacterial secondary metabolite toxic to humans and other living organisms. Strain OF001 and A210 are manganese-oxidizing bacteria (MOB) able to transform cylindrospermopsin during the oxidation of Mn2+. So far, the enzymes involved in manganese oxidation in strain OF001 and A210 are unknown. Therefore, we analyze the genomes of two cylindrospermopsin-transforming MOB, Pseudomonas sp. OF001 and Rubrivivax sp. A210, to identify enzymes that could catalyze the oxidation of Mn2+. We also investigated specific metabolic features related to pollutant degradation and explored the metabolic potential of these two MOB with respect to the role they may play in biotechnological applications and/or in the environment. Results Strain OF001 encodes two multicopper oxidases and one haem peroxidase potentially involved in Mn2+ oxidation, with a high similarity to manganese-oxidizing enzymes described for Pseudomonas putida GB-1 (80, 83 and 42% respectively). Strain A210 encodes one multicopper oxidase potentially involved in Mn2+ oxidation, with a high similarity (59%) to the manganese-oxidizing multicopper oxidase in Leptothrix discophora SS-1. Strain OF001 and A210 have genes that might confer them the ability to remove aromatic compounds via the catechol meta- and ortho-cleavage pathway, respectively. Based on the genomic content, both strains may grow over a wide range of O2 concentrations, including microaerophilic conditions, fix nitrogen, and reduce nitrate and sulfate in an assimilatory fashion. Moreover, the strain A210 encodes genes which may convey the ability to reduce nitrate in a dissimilatory manner, and fix carbon via the Calvin cycle. Both MOB encode CRISPR-Cas systems, several predicted genomic islands, and phage proteins, which likely contribute to their genome plasticity. Conclusions The genomes of Pseudomonas sp. OF001 and Rubrivivax sp. A210 encode sequences with high similarity to already described MCOs which may catalyze manganese oxidation required for cylindrospermopsin transformation. Furthermore, the analysis of the general metabolism of two MOB strains may contribute to a better understanding of the niches of cylindrospermopsin-removing MOB in natural habitats and their implementation in biotechnological applications to treat water.

scholarly journals Mn(II) Oxidation by the Multicopper Oxidase Complex Mnx: A Coordinated Two-Stage Mn(II)/(III) and Mn(III)/(IV) Mechanism

2017 ◽  
Vol 139 (33) ◽  
pp. 11381-11391 ◽  
Author(s):  
Alexandra V. Soldatova ◽  
Christine A. Romano ◽  
Lizhi Tao ◽  
Troy A. Stich ◽  
William H. Casey ◽  
...  
Keyword(s):  
Multicopper Oxidase ◽  
Two Stage

scholarly journals The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO fromE. coli

Metallomics ◽  
2015 ◽  
Vol 7 (5) ◽  
pp. 776-785 ◽  
Author(s):  
Laura Cortes ◽  
Anthony G. Wedd ◽  
Zhiguang Xiao
Keyword(s):  
Oxidase Activity ◽  
Multicopper Oxidase ◽  
Functional Roles ◽  
E Coli ◽  
Copper Sites

The methionine-rich insert in the multicopper oxidase CueO fromE. coliaccommodates three copper sites that play distinct but related roles in Cu(i) extraction and oxidation and that induce robust cuprous oxidase activity under physiologically relevant conditions.

Spectroscopic Characterization and O2Reactivity of the Trinuclear Cu Cluster of Mutants of the Multicopper Oxidase Fet3p†

Biochemistry ◽  
2002 ◽  
Vol 41 (20) ◽  
pp. 6438-6448 ◽  
Author(s):  
Amy E. Palmer ◽  
Liliana Quintanar ◽  
Scott Severance ◽  
Tzu-Pin Wang ◽  
Daniel J. Kosman ◽  
...  
Keyword(s):  
Spectroscopic Characterization ◽  
Multicopper Oxidase

Metallo-inhibition of Mnx, a bacterial manganese multicopper oxidase complex

2021 ◽  
pp. 111547
Author(s):  
Alexandra V. Soldatova ◽  
Wen Fu ◽  
Christine A. Romano ◽  
Lizhi Tao ◽  
William H. Casey ◽  
...  
Keyword(s):  
Multicopper Oxidase
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