Quinoproteins: structure, function, and biotechnological applications

Matsushita, Kazunobu; Toyama, Hirohide; Yamada, Mamoru; Adachi, Osao

doi:10.1007/s00253-001-0851-1

Cited by 134 publications

(19 citation statements)

References 31 publications

(47 reference statements)

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“…PQQ is a prosthetic group utilized by some bacterial dehydrogenases (121). In these quinoproteins, PQQ binds to the center of a disc-like structure created by the β-propeller folds and is a co-factor in oxido-reduction reactions (54).…”

Section: Structure and Function Of The Bam Complexmentioning

confidence: 99%

Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex

Malinverni

Silhavy

2011

EcoSal Plus

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The major class of integral proteins found in the outer membrane (OM) of E. coli and Salmonella adopt a β-barrel conformation (OMPs). OMPs are synthesized in the cytoplasm with a typical signal sequence at the amino terminus, which directs them to the secretion machinery (SecYEG) located in the inner membrane for translocation to the periplasm. Chaperones such as SurA, or DegP and Skp, escort these proteins across the aqueous periplasm protecting them from aggregation. The chaperones then deliver OMPs to a highly conserved outer membrane assembly site termed the Bam complex. In E. coli , the Bam complex is composed of an essential OMP, BamA, and four associated OM lipoproteins, BamBCDE, one of which, BamD, is also essential. Here we provide an overview of what we know about the process of OMP assembly and outline the various hypotheses that have been proposed to explain how proteins might be integrated into the asymmetric OM lipid bilayer in an environment that lacks obvious energy sources. In addition, we describe the envelope stress responses that ensure the fidelity of OM biogenesis and how factors, such as phage and certain toxins, have coopted this essential machine to gain entry into the cell.

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Section: Structure and Function Of The Bam Complexmentioning

confidence: 99%

Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex

Malinverni

Silhavy

2011

EcoSal Plus

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“…Some prokaryotic organisms are able to synthesize PQQ, whereas others require an exogenous source. The enzyme group to which the PQQ cofactor belongs is the quinoprotein group [3]–[5], and all PQQ-dependent quinoproteins reported to date have a characteristic propeller-fold superbarrel structure [3], [5]. Bacterial PQQ-dependent dehydrogenases which have an eight-bladed structure contain the characteristic amino acid sequence, which has been usually used to identify PQQ-dependent proteins.…”

Section: Introductionmentioning

confidence: 99%

Discovery of a Eukaryotic Pyrroloquinoline Quinone-Dependent Oxidoreductase Belonging to a New Auxiliary Activity Family in the Database of Carbohydrate-Active Enzymes

et al. 2014

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Pyrroloquinoline quinone (PQQ) is a redox cofactor utilized by a number of prokaryotic dehydrogenases. Not all prokaryotic organisms are capable of synthesizing PQQ, even though it plays important roles in the growth and development of many organisms, including humans. The existence of PQQ-dependent enzymes in eukaryotes has been suggested based on homology studies or the presence of PQQ-binding motifs, but there has been no evidence that such enzymes utilize PQQ as a redox cofactor. However, during our studies of hemoproteins, we fortuitously discovered a novel PQQ-dependent sugar oxidoreductase in a mushroom, the basidiomycete Coprinopsis cinerea. The enzyme protein has a signal peptide for extracellular secretion and a domain for adsorption on cellulose, in addition to the PQQ-dependent sugar dehydrogenase and cytochrome domains. Although this enzyme shows low amino acid sequence homology with known PQQ-dependent enzymes, it strongly binds PQQ and shows PQQ-dependent activity. BLAST search uncovered the existence of many genes encoding homologous proteins in bacteria, archaea, amoebozoa, and fungi, and phylogenetic analysis suggested that these quinoproteins may be members of a new family that is widely distributed not only in prokaryotes, but also in eukaryotes.

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“…Kasahara and Kato previously identified U26 as a potential PQQ-dependent enzyme, containing a putative PQQ-binding motif, in mice and observed that the enzyme could be involved in the metabolic degradation of dietary lysine, acting as a PQQ-dependent 2-aminoadipic 6-semialdehyde dehydrogenase (AASDH)10. Because all bacterial PQQ-dependent dehydrogenases reported to date have a characteristic consensus structure, PQQ-binding β-propeller motif, for PQQ-dependent proteins41112, they concluded PQQ to be a newcomer to the B group of vitamins. However, the claim for a mammalian vitamin was subsequently questioned by other scientists because no PQQ-dependent AASDH activity was detected in mammalian tissues either in vivo or in vitro , and U26-dependent oxidation of 2-aminoadipate semialdehyde to 2-aminoadipate has never been experimentally demonstrated131415.…”

mentioning

confidence: 99%

Identification of lactate dehydrogenase as a mammalian pyrroloquinoline quinone (PQQ)-binding protein

Akagawa

Minematsu

Shibata

et al. 2016

Sci Rep

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Pyrroloquinoline quinone (PQQ), a redox-active o-quinone, is an important nutrient involved in numerous physiological and biochemical processes in mammals. Despite such beneficial functions, the underlying molecular mechanisms remain to be established. In the present study, using PQQ-immobilized Sepharose beads as a probe, we examined the presence of protein(s) that are capable of binding PQQ in mouse NIH/3T3 fibroblasts and identified five cellular proteins, including l-lactate dehydrogenase (LDH) A chain, as potential mammalian PQQ-binding proteins. In vitro studies using a purified rabbit muscle LDH show that PQQ inhibits the formation of lactate from pyruvate in the presence of NADH (forward reaction), whereas it enhances the conversion of lactate to pyruvate in the presence of NAD+ (reverse reaction). The molecular mechanism underlying PQQ-mediated regulation of LDH activity is attributed to the oxidation of NADH to NAD+ by PQQ. Indeed, the PQQ-bound LDH oxidizes NADH, generating NAD+, and significantly catalyzes the conversion of lactate to pyruvate. Furthermore, PQQ attenuates cellular lactate release and increases intracellular ATP levels in the NIH/3T3 fibroblasts. Our results suggest that PQQ, modulating LDH activity to facilitate pyruvate formation through its redox-cycling activity, may be involved in the enhanced energy production via mitochondrial TCA cycle and oxidative phosphorylation.

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Quinoproteins: structure, function, and biotechnological applications

Cited by 134 publications

References 31 publications

Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex

Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex

Discovery of a Eukaryotic Pyrroloquinoline Quinone-Dependent Oxidoreductase Belonging to a New Auxiliary Activity Family in the Database of Carbohydrate-Active Enzymes

Identification of lactate dehydrogenase as a mammalian pyrroloquinoline quinone (PQQ)-binding protein

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