On the structure and linkage of the covalent cofactor of methylamine dehydrogenase from the methylotrophic bacterium W3A1

doi:10.1016/S0006-291X(86)80210-8

Biochemical and Biophysical Research Communications

Volume 141, Issue 2, 15 December 1986, Pages 562-568

https://doi.org/10.1016/S0006-291X(86)80210-8 Get rights and content

Short amino acid sequences around the two linkage sites of the cofactor of methylamine dehydrogenase are presented. Mass spectral data indicates that the covalently bound cofactor is the tricylic pyrroloquinoline quinone (PQQ). However, the 3 carboxyl groups characteristic of this o-quinone are absent. A cysteine thioether, via a methylene bridge, and a serine ether link the cofactor to the small subunit of methylamine dehydrogenase.

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Cited by (35)

Tryptophan tryptophylquinone in bacterial amine dehydrogenases
1995, Methods in Enzymology
Separation of amino acid-oxazole derivatives of the redox coenzyme pyrroloquinoline quinone by capillary zone electrophoresis
1993, Journal of Chromatography A
Condensation products (oxazole derivatives) from the reaction of the coenzyme pyrroloquinoline quinone (PQQ) with several α-amino acids were successfully separated by capillary zone electrophoresis. Addition of a certain organic solvent such as dimethyl sulphoxide to the electrolyte solution is essential for reproducible and complete separation. The organic modifier appears to prevent the oxazole derivatives from adsorbing on the capillary wall. Product analysis of the condensation reactions of PQQ with amino acids was performed by this method and the mechanism is discussed briefly. PQQ-spiked bovine serum was also analysed. Unsubstituted type 1 oxazole derivative was predominantly detected. This result suggests that most of the PQQ in mammalian fluids, if any, exists as PQQ derivatives, probably as a type 1 oxazole derivative.
Surprises among quinoproteins. Current Opinion in Structural Biology 1991, 1:968-972
1991, Current Opinion in Structural Biology
Until recently, pyrroloquinoline quinone had been attributed the role of redox cofactor for a wide range of prokaryotic and eukaryotic enzymes. A well delineated function for pyrroloquinoline quinone now appears to be limited to prokaryotes, where it acts as a dissociable redox cofactor. Advances during the past 18 months include the identification of two new covalently bound quinone cofactors: topa quinone and tryptophan tryptophylquinone. These structures are generated in mammals and bacteria, respectively, via the post-translational processing of existing protein side chains.
Mechanism of amine oxidation by coenzyme PQQ
1991, Bioorganic Chemistry
Chemical behavior of coenzyme PQQ and its analogues toward several amines is reviewed. Product analyses and kinetic studies so far reported indicate that the oxidation of primary amines by pyrroloquinoline quinone derivatives proceeds via the ionic mechanism through the carbinolamine intermediate from which two competing reaction pathways, direct α-proton abstraction and transamination, occur to give the quinol and the aminophenol products, respectively. The similar ionic mechanism through the carbinolamine-type intermediate is proposed for the reactions between PQQ and α,ϵ-diaminoalkanes, hydrazines, and aminoguanidine, where the redox reaction (quinol formation) and adduct formation reactions are controlled by alkylene chain length, electronic nature of the substituents, and pH conditions of the solution, respectively. PQQ catalyzes oxidative decarboxylation and oxidative dealdolation (C_αC_β bond fission) of α-amino acids, which can be also interpreted by the similar ionic mechaism.
Microbial metabolism of C<inf>1</inf>-nitrogen compounds other than cyanide
1990, FEMS Microbiology Letters
The following topics are discussed in this review: the structure of methylamine dehydrogenase and the binding of its pyrrolo-quinoline quinone (PQQ) prosthetic group, the role of the copper protein amicyanin as electron acceptor of the enzyme and the nature of the electron carriers between amicyanin and oxygen in the electron transport chain. Also covered are recent developments in the metabolism of trimethylamine and its N-oxide and N-methylformamides.
The role of PQQ and quinoproteins in methylotrophic bacteria
1990, FEMS Microbiology Letters
Quinoprotein dehydrogenases play a non-exclusive role in the dissimilation of C₁ compounds. Methanol and methylamine oxidation occur by covalent catalysis while the reduction equivalents are transferred to the respiratory chain in one-electron steps. Cytochrome c_L is an excellent electron acceptor for methanol dehydrogenase at pH 7.0 and a bad one at pH 9.0. Efficient methanol oxidation (with NH₃ as activator) occurs at pH 9.0, but (due to the failure of NH₃) not at pH 7.0. Since stimulation occurred at the latter condition with a compound prepared from Hyphomicrobium X, most probably methanol oxidation in vivo requires the presence of a natural activator. The finding of pro-PQQ in methylamine dehydrogenase implicates that certain quinoproteins may have a modified tyrosine as cofactor. This type of quinoprotein is involved in assimilation routes which also occur in methylotrophs. l-Tyrosine and l-glutamate are the precursors of PQQ biosynthesis. Free intermediates in the route of biosynthesis have not been found. Most probably the whole process occurs on a protein matrix. In view of the significant amounts found in their culture fluid, methylotrophic bacteria seem particularly well suited for the fermentative production of PQQ.

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On the structure and linkage of the covalent cofactor of methylamine dehydrogenase from the methylotrophic bacterium W3A1

FEMS Microbiol. Rev.

Agric. Biol. Chem.

Agric. Biol. Chem.

Agric. Biol. Chem.

Chem. Abst.

FEBS Lett.