Pyrroloquinoline Quinone-Dependent Cytochrome Reduction in Polyvinyl Alcohol-Degrading
            <i>Pseudomonas</i>
            sp. Strain VM15C

Shimao, Masayuki; Onishi, Syuji; Kato, Nobuo; Sakazawa, Chikahiro

doi:10.1128/aem.55.2.275-278.1989

Cited by 20 publications

(2 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…113P3 (14), which is a primary electron acceptor for PVADHs in PVA oxidation ( Fig. 2A) (19,34). We predict that BAY15_1712, BAY15_2325 (oxidation), and BAY15_0291 (electron acceptor) may work together to implement the first step of the oxidation of PVA in S. rhizophila QL-P4 (Fig.…”

Section: Figmentioning

confidence: 92%

Bioinformatics Analysis and Characterization of Highly Efficient Polyvinyl Alcohol (PVA)-Degrading Enzymes from the Novel PVA Degrader Stenotrophomonas rhizophila QL-P4

Wei¹,

Wu³

et al. 2018

Appl Environ Microbiol

View full text Add to dashboard Cite

Polyvinyl alcohol (PVA) is used widely in industry, and associated environmental pollution is a serious problem. Herein, we report a novel, efficient PVA degrader, QL-P4, isolated from fallen leaves from a virgin forest in the Qinling Mountains. The complete genome was obtained using single-molecule real-time (SMRT) technology and corrected using Illumina sequencing. Bioinformatics analysis revealed eight PVA/vinyl alcohol oligomer (OVA)-degrading genes. Of these, seven genes were predicted to be involved in the classic intracellular PVA/OVA degradation pathway, and one (BAY15_3292) was identified as a novel PVA oxidase. Five PVA/OVA-degrading enzymes were purified and characterized. One of these, BAY15_1712, a PVA dehydrogenase (PVADH), displayed high catalytic efficiency toward PVA and OVA substrate. All reported PVADHs only have PVA-degrading ability. Most importantly, we discovered a novel PVA oxidase (BAY15_3292) that exhibited higher PVA-degrading efficiency than the reported PVADHs. Further investigation indicated that BAY15_3292 plays a crucial role in PVA degradation in QL-P4. Knocking out BAY15_3292 resulted in a significant decline in PVA-degrading activity in QL-P4. Interestingly, we found that BAY15_3292 possesses exocrine activity, which distinguishes it from classic PVADHs. Transparent circle experiments further proved that BAY15_3292 greatly affects extracellular PVA degradation in QL-P4. The exocrine characteristics of BAY15_3292 facilitate its potential application to PVA bioremediation. In addition, we report three new efficient secondary alcohol dehydrogenases (SADHs) with OVA-degrading ability in QL-P4; in contrast, only one OVA-degrading SADH was reported previously. With the widespread application of PVA in industry, PVA-related environmental pollution is an increasingly serious issue. Because PVA is difficult to degrade, it accumulates in aquatic environments and causes chronic toxicity to aquatic organisms. Biodegradation of PVA, as an economical and environment-friendly method, has attracted much interest. To date, effective and applicable PVA-degrading bacteria/enzymes have not been reported. Herein, we report a new efficient PVA degrader ( QL-P4) that has five PVA/OVA-degrading enzymes with high catalytic efficiency, among which BAY15_1712 is the only reported PVADH with both PVA- and OVA-degrading abilities. Importantly, we discovered a novel PVA oxidase (BAY15_3292) that is not only more efficient than other reported PVA-degrading PVADHs but also has exocrine activity. Overall, our findings provide new insight into PVA-degrading pathways in microorganisms and suggest QL-P4 and its enzymes have the potential for application to PVA bioremediation to reduce or eliminate PVA-related environmental pollution.

show abstract

Section: Figmentioning

confidence: 92%

Bioinformatics Analysis and Characterization of Highly Efficient Polyvinyl Alcohol (PVA)-Degrading Enzymes from the Novel PVA Degrader Stenotrophomonas rhizophila QL-P4

Wei¹,

Wu³

et al. 2018

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…These enzymes are predominantly found in Gram-negative bacteria, where they are localized to the periplasm and are sometimes membrane-associated 1 . The periplasmic localization of quinoproteins allows for the oxidation of catabolic substrates without their import into the cytoplasm, with the resulting electrons delivered to the respiratory chain via the reduction of C-type cytochromes, membrane-bound respiratory quinones, or azurin 1,9,11,12 .…”

Section: Introductionmentioning

confidence: 99%

High-affinity PQQ import is widespread in Gram-negative bacteria

Munder,

Voutsinos,

Hantke

et al. 2024

Preprint

View full text Add to dashboard Cite

PQQ is a soluble redox cofactor used by diverse bacteria to oxidise fuel compounds as a source of electrons for the respiratory chain. Many Gram-negative bacteria that encode PQQ-dependent enzymes do not possess the biosynthetic machinery for its production and instead obtain it from the environment. To achieve this the bacteriumEscherichia coliuses the TonB-dependent transporter PqqU as a high-affinity PQQ importer, allowing it to use PQQ at an external concentration as low as 1 nM. Here, we show that PqqU achieves this by binding PQQ with a very high affinity. Using cryo-electron microscopy we determine the structure of the PqqU-PQQ complex at a resolution of 1.99 Å, revealing that the extracellular loops of PqqU undergo significant conformational changes upon PQQ binding, which captures the cofactor in an internal cavity. This cavity likely facilitates an airlock-style gating mechanism that prevents non-specific import through PqqU. Using structural modelling we show that the change in PqqU structure upon PQQ binding precludes the binding of bacteriophage, which targets it as a cell surface receptor. Guided by the PqqU-PQQ complex structure we use phenotypic analysis to identify the amino acids essential for PQQ import and leverage this information to map the presence of PqqU across Gram-negative bacteria. This reveals that PqqU is encoded by Gram-negative bacteria from at least 22 phyla from diverse habitats, including those found in aquatic, soil, host-associated, and extreme environments. This indicates that PQQ is a ubiquitous nutrient in many environments, and an important cofactor for bacteria that adopt diverse lifestyles and metabolic strategies.Significance StatementMany enzymes form complexes with molecules called cofactors to perform their function. PQQ is a cofactor used by bacterial enzymes that provide energy by breaking down food molecules. While some bacteria make their own PQQ, other bacteria use the transport protein PqqU to bind PQQ from the environment and import it into their cells. We show that PqqU binds PQQ very tightly, allowing bacteria to acquire it at very low concentrations. Using cryo-electron microscopy we image the PqqU-PQQ complex on an atomic level, revealing how PQQ is bound so tightly. Using this the information to analyse microbial genomes, we show that PQQ scavenging is employed by diverse bacteria, implying that PQQ is an important common good of diverse microbiomes.

show abstract

Biodegradation of Poly(vinyl alcohol) and its Copolymers

Matsumura

2002

Biopolymers Online

View full text Add to dashboard Cite

Introduction Historical Outline Chemical Structures Functions Physical Properties Properties of PVA film Properties of Aqueous PVA Solution Chemical Properties of PVA Physiology and Biochemistry Biodegradation Microbial Degradation of PVA and Related Enzymes PVA Biodegradation Mechanism and Related Enzymes Polymer Structure and Biodegradation Biodegradation of PVA‐based Polymer Design of Biodegradable Polymer using Vinyl Alcohol Block Production Outlook and Perspectives Patents Acknowledgments

show abstract

Pyrroloquinoline Quinone-Dependent Cytochrome Reduction in Polyvinyl Alcohol-Degrading Pseudomonas sp. Strain VM15C

Cited by 20 publications

References 15 publications

Bioinformatics Analysis and Characterization of Highly Efficient Polyvinyl Alcohol (PVA)-Degrading Enzymes from the Novel PVA Degrader Stenotrophomonas rhizophila QL-P4

Bioinformatics Analysis and Characterization of Highly Efficient Polyvinyl Alcohol (PVA)-Degrading Enzymes from the Novel PVA Degrader Stenotrophomonas rhizophila QL-P4

High-affinity PQQ import is widespread in Gram-negative bacteria

Biodegradation of Poly(vinyl alcohol) and its Copolymers

Contact Info

Product

Resources

About