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Titel
The pyrroloquinoline quinone biosynthesis pathway revisited : a structural approach
VerfasserPuehringer, Sandra ; Metlitzky, Moritz ; Schwarzenbacher, Robert
Erschienen in
BMC Biochemistry, London, 2009, Jg. 9, H. 8, S. 1-10
ErschienenBioMed Central, 2009
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
ISSN1471-2091
URNurn:nbn:at:at-ubs:3-6103 Persistent Identifier (URN)
DOI10.1186/1471-2091-9-8 
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The pyrroloquinoline quinone biosynthesis pathway revisited [7.03 mb]
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Background: 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. Results: New 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. Conclusion: PQQ 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.