![]() |
|
PROSITE documentation PDOC00375 [for PROSITE entry PS00364] |
Pyrrolo-quinoline quinone (PQQ) is redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [1,2]. A number of these bacterial quinoproteins are clearly evolutionary related. These proteins are listed below.
These dehydrogenases all have from 600 to 800 amino acids. We developed two signature patterns for these proteins using sequence data from well conserved regions: the first one is located in the N-terminal half while the second one is from the C-terminal half.
Last update:December 2004 / Patterns and text revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Duine J.A. Jongejan J.A. |
Title | Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor. | |
Source | Annu. Rev. Biochem. 58:403-426(1989). | |
PubMed ID | 2549854 | |
DOI | 10.1146/annurev.bi.58.070189.002155 |
2 | Authors | Gallop P.M. Paz M.A. Flueckiger R. Kagan H.M. |
Title | PQQ, the elusive coenzyme. | |
Source | Trends Biochem. Sci. 14:343-346(1989). | |
PubMed ID | 2572081 |
3 | Authors | Inoue T. Sunagawa M. Mori A. Imai C. Fukuda M. Takagi M. Yano K. |
Title | Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti. | |
Source | J. Bacteriol. 171:3115-3122(1989). | |
PubMed ID | 2722742 |
4 | Authors | Cleton-Jansen A.-M. Dekker S. van de Putte P. Goosen N. |
Source | Mol. Gen. Genet. 229:206-212(1991). |