Abstract
BackgroundThe biosynthesis pathway of Pyrroloquinoline quinone, a bacterial redox active cofactor for numerous alcohol and aldose dehydrogenases, is largely unknown, but it is proven that at least six genes in Klebsiella pneumoniae (PqqA-F) are required, all of which are located in the PQQ-operon.ResultsNew structural data of some PQQ biosynthesis proteins and their homologues provide new insights and functional assignments of the proteins in the pathway. Based on sequence analysis and homology models we propose the role and catalytic function for each enzyme involved in this intriguing biosynthesis pathway.ConclusionPQQ is derived from the two amino acids glutamate and tyrosine encoded in the precursor peptide PqqA. Five reactions are necessary to form this quinone cofactor. The PqqA peptide is recognised by PqqE, which links the C9 and C9a, afterwards it is accepted by PqqF which cuts out the linked amino acids. The next reaction (Schiff base) is spontaneous, the following dioxygenation is catalysed by an unknown enzyme. The last cyclization and oxidation steps are catalysed by PqqC. Taken together the known facts of the different proteins we assign a putative function to all six proteins in PQQ biosynthesis pathway.
Highlights
The biosynthesis pathway of Pyrroloquinoline quinone, a bacterial redox active cofactor for numerous alcohol and aldose dehydrogenases, is largely unknown, but it is proven that at least six genes in Klebsiella pneumoniae (PqqA-F) are required, all of which are located in the PQQ-operon
PQQ is derived from the two amino acids glutamate and tyrosine encoded in the precursor peptide PqqA
The PqqA peptide is recognised by PqqE, which links the C9 and C9a, afterwards it is accepted by PqqF which cuts out the linked amino acids
Summary
The biosynthesis pathway of Pyrroloquinoline quinone, a bacterial redox active cofactor for numerous alcohol and aldose dehydrogenases, is largely unknown, but it is proven that at least six genes in Klebsiella pneumoniae (PqqA-F) are required, all of which are located in the PQQ-operon. Pyrroloquinoline quinone (4,5-dihydro-4,5-dioxo-1Hpyrrolo-[2,3-f]quinoline-2,7,9-tricarboxylic acid: PQQ) is a water soluble, heat-stable, tricyclic ortho-quinone. It serves as redox cofactor for various bacterial dehydrogenases[1] providing unique redox-features. PQQ was the first cofactor to be found in this cofactor-family, followed by the identification of tryptophan tryptophylquinone (TTQ), trihydroxyphenylalanyl quinone (topaquinone or TPQ), lysine tyrosylquinone (LTQ) and the copper-complexed cysteinyltyrosyl radical. This family is the third family of cofactors following pyridine nucleotide- and flavin-dependent cofactors [5]. PQQ has provoked significant additional interest because of its presence in foods, its antioxidant properties and its (page number not for citation purposes)
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