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Revision as of 12:14, 6 December 2011 editBeetstra (talk | contribs)Edit filter managers, Administrators172,031 edits Saving copy of the {{chembox}} taken from revid 458781160 of page Pyrroloquinoline_quinone for the Chem/Drugbox validation project (updated: 'CASNo').  Latest revision as of 01:54, 1 January 2025 edit Arthurfragoso (talk | contribs)Extended confirmed users2,108 edits Fixes image in dark mode 
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{{Use dmy dates|date=March 2023}}
{{ambox | text = This page contains a copy of the infobox ({{tl|chembox}}) taken from revid of page ] with values updated to verified values.}}
{{chembox {{chembox
| Verifiedfields = changed
⚫ | verifiedrevid = 450487783
| Watchedfields = changed
⚫ | verifiedrevid = 464377908
| ImageFile_Ref = {{chemboximage|correct|??}} | ImageFile_Ref = {{chemboximage|correct|??}}
| ImageFile=Pyrroloquinoline quinone.svg | ImageFile=Pyrroloquinoline quinone.svg
| ImageClass=skin-invert-image
|ImageSize= | ImageSize=
|IUPACName=
| SystematicName=4,5-Dioxo-4,5-dihydro-1''H''-pyrroloquinoline-2,7,9-tricarboxylic acid
|OtherNames= | OtherNames=
|Section1= {{Chembox Identifiers |Section1={{Chembox Identifiers
⚫ | KEGG_Ref = {{keggcite|correct|kegg}}
⚫ | CASNo_Ref = {{cascite|correct|cas}}
| CASNo=72909-34-3
| Beilstein = 3596812
⚫ | ChEBI_Ref = {{ebicite|correct|EBI}}
⚫ | ChEBI = 18315
| ChEMBL = 1235421
⚫ | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
⚫ | ChemSpiderID = 997
| DrugBank = DB03205
| EC_number = 839-691-6
| Gmelin = 56633
⚫ | KEGG_Ref = {{keggcite|correct|kegg}}
| KEGG = C00113 | KEGG = C00113
⚫ | PubChem=1024
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = 47819QGH5L
| InChI = 1/C14H6N2O8/c17-10-4-2-6(14(23)24)15-8(4)7-3(12(19)20)1-5(13(21)22)16-9(7)11(10)18/h1-2,15H,(H,19,20)(H,21,22)(H,23,24) | InChI = 1/C14H6N2O8/c17-10-4-2-6(14(23)24)15-8(4)7-3(12(19)20)1-5(13(21)22)16-9(7)11(10)18/h1-2,15H,(H,19,20)(H,21,22)(H,23,24)
| InChIKey = MMXZSJMASHPLLR-UHFFFAOYAP | InChIKey = MMXZSJMASHPLLR-UHFFFAOYAP
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| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} | StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = MMXZSJMASHPLLR-UHFFFAOYSA-N | StdInChIKey = MMXZSJMASHPLLR-UHFFFAOYSA-N
⚫ | CASNo_Ref = {{cascite|correct|??}}
| CASNo = <!-- blanked - oldvalue: 72909-34-3 -->
⚫ | PubChem=1024
⚫ | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
⚫ | ChemSpiderID = 997
⚫ | ChEBI_Ref = {{ebicite|correct|EBI}}
⚫ | ChEBI = 18315
| SMILES = c1c2c(c1C(=O)O)-c3c(cc(nc3C(=O)C2=O)C(=O)O)C(=O)O | SMILES = c1c2c(c1C(=O)O)-c3c(cc(nc3C(=O)C2=O)C(=O)O)C(=O)O
| MeSHName=PQQ+Cofactor | MeSHName=PQQ+Cofactor
}} }}
|Section2= {{Chembox Properties |Section2={{Chembox Properties
| C=14 | H=6 | N=2 | O=8
| Formula=C<sub>14</sub>H<sub>6</sub>N<sub>2</sub>O<sub>8</sub>
⚫ | Appearance=
| MolarMass=330.206 g/mol
⚫ | Density=1.963 g/cm<sup>3</sup>
⚫ | Appearance=
| MeltingPt=
⚫ | Density=1.963g/cm<sup>3</sup>
| MeltingPt= | BoilingPt=
⚫ | Solubility=
| BoilingPt=1018.6°C @ 760mmHg
⚫ | Solubility=
}} }}
|Section3= {{Chembox Hazards |Section3={{Chembox Hazards
| MainHazards= | MainHazards=
| FlashPt=569.8°C | FlashPtC = 569.8
| AutoignitionPtC =
| Autoignition=
}} }}
}} }}

'''Pyrroloquinoline quinone''' ('''PQQ'''), also called '''methoxatin''''','' is a ] and ].<ref>Wen H, He Y, Zhang K, Yang X, Hao D, Jiang Y, He B. Mini-review: Functions and Action Mechanisms of PQQ in Osteoporosis and Neuro Injury. ''Curr Stem Cell Res Ther''. 2020;15(1):32-36. {{doi|10.2174/1574888X14666181210165539}} {{PMID|30526470}}</ref>

] is used as a glucose sensor in bacteria. PQQ stimulates growth in bacteria.<ref>{{Cite journal |vauthors=Ameyama M, Matsushita K, Shinagawa E, Hayashi M, Adachi O |year=1988 |title=Pyrroloquinoline quinone: excretion by methylotrophs and growth stimulation for microorganisms |journal=BioFactors |volume=1 |issue=1 |pages=51–3 |pmid=2855583}}</ref>

== History ==
It was discovered by J. G. Hauge as the third ] after ] and ] in bacteria (although he hypothesised that it was ]).<ref>{{Cite journal |last=Hauge JG |year=1964 |title=Glucose dehydrogenase of bacterium anitratum: an enzyme with a novel prosthetic group |journal=J Biol Chem |volume=239 |issue=11 |pages=3630–9 |doi=10.1016/S0021-9258(18)91183-X |pmid=14257587 |doi-access=free}}</ref> Anthony and Zatman also found the unknown redox cofactor in ]. In 1979, Salisbury and colleagues<ref>{{Cite journal |vauthors=Salisbury SA, Forrest HS, Cruse WB, Kennard O |year=1979 |title=A novel coenzyme from bacterial primary alcohol dehydrogenases |journal=Nature |volume=280 |issue=5725 |pages=843–4 |bibcode=1979Natur.280..843S |doi=10.1038/280843a0 |pmid=471057 |s2cid=3094647}}</ref> as well as Duine and colleagues<ref>{{Cite journal |vauthors=Westerling J, Frank J, Duine JA |year=1979 |title=The prosthetic group of methanol dehydrogenase from Hyphomicrobium X: electron spin resonance evidence for a quinone structure |journal=Biochem Biophys Res Commun |volume=87 |issue=3 |pages=719–24 |doi=10.1016/0006-291X(79)92018-7 |pmid=222269}}</ref> extracted this ] from ] of ]s and identified its molecular structure. Adachi and colleagues discovered that PQQ was also found in '']''.<ref>{{Cite journal |vauthors=Ameyama M, Matsushita K, Ohno Y, Shinagawa E, Adachi O |year=1981 |title=Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria |journal=FEBS Lett |volume=130 |issue=2 |pages=179–83 |doi=10.1016/0014-5793(81)81114-3 |pmid=6793395 |doi-access=free}}</ref>

== Biosynthesis ==
{{further|Ribosomally synthesized and post-translationally modified peptides}}
A novel aspect of PQQ is its biosynthesis in bacteria from a ribosomally translated precursor peptide, PqqA (] {{UniProt|P27532}}).<ref name="pmid1310505">{{Cite journal |vauthors=Goosen N, Huinen RG, van de Putte P |year=1992 |title=A 24-amino-acid polypeptide is essential for the biosynthesis of the coenzyme pyrrolo-quinoline-quinone. |journal=J Bacteriol |volume=174 |issue=4 |pages=1426–7 |doi=10.1128/jb.174.4.1426-1427.1992 |pmc=206443 |pmid=1310505}}</ref> A ] and a ] in PqqA are cross-linked by the ] ] PqqE ({{UniProt|P07782}}) with the help of PqqD ({{UniProt|P07781}}) in the first step of PqqA modification.<ref name="pmid21223593" /> A protease then liberates the Glu-Tyr molecule from the peptide backbone. PqqB ({{UniProt|P07779}}) oxidizes the 2 and 3 positions on the tyrosine ring, forming a quinone which quickly becomes AHQQ, finishing the ] ring. PqqC ({{UniProt|P07780}}) then forms the final ] ring.<ref name="pmid32731194">{{Cite journal |last1=Zhu |first1=W |last2=Klinman |first2=JP |date=December 2020 |title=Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone. |journal=Current Opinion in Chemical Biology |volume=59 |pages=93–103 |doi=10.1016/j.cbpa.2020.05.001 |pmc=7736144 |pmid=32731194}}</ref>

Efforts to understand PQQ biosynthesis have contributed to broad interest in radical SAM enzymes and their ability to modify proteins, and an analogous radical SAM enzyme-dependent pathway has since been found that produces the putative electron carrier ], using a ] and a ] from the precursor peptide, MftA ({{UniProt|P9WJ81}}).<ref name="pmid21223593">{{Cite journal |last=Haft DH |year=2011 |title=Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners. |journal=BMC Genomics |volume=12 |pages=21 |doi=10.1186/1471-2164-12-21 |pmc=3023750 |pmid=21223593 |doi-access=free }}</ref>

== Role in proteins ==
Quinoproteins generally embed the cofactor in a unique, six-bladed<ref name="pmid31604769"/> ] structure. Some examples also have a ] prosthetic group and are termed quinohemoproteins.<ref>{{Cite journal |last1=Matsushita |first1=K |last2=Toyama |first2=H |last3=Yamada |first3=M |last4=Adachi |first4=O |date=January 2002 |title=Quinoproteins: structure, function, and biotechnological applications. |journal=Applied Microbiology and Biotechnology |volume=58 |issue=1 |pages=13–22 |doi=10.1007/s00253-001-0851-1 |pmid=11831471 |s2cid=12469203}}</ref> Although quinoproteins are mostly found in bacteria, a '']'' (fungus) ] has been shown to use PQQ in its crystal structure.<ref name="pmid31604769">{{Cite journal |last1=Takeda |first1=K |last2=Ishida |first2=T |last3=Yoshida |first3=M |last4=Samejima |first4=M |last5=Ohno |first5=H |last6=Igarashi |first6=K |last7=Nakamura |first7=N |date=15 December 2019 |title=Crystal Structure of the Catalytic and Cytochrome ''b'' Domains in a Eukaryotic Pyrroloquinoline Quinone-Dependent Dehydrogenase. |journal=Applied and Environmental Microbiology |volume=85 |issue=24 |bibcode=2019ApEnM..85E1692T |doi=10.1128/AEM.01692-19 |pmc=6881789 |pmid=31604769 |doi-access=free}}</ref>

PQQ also appears to be essential in some other eukaryotic proteins, albeit not as the direct electron carrier. The mammalian ] requires PQQ to run but uses ] as the direct redox cofactor. It seems to speed up the reaction by catalyzing the oxidation of NADH via redox cycling.<ref>{{Cite journal |last1=Akagawa |first1=M |last2=Minematsu |first2=K |last3=Shibata |first3=T |last4=Kondo |first4=T |last5=Ishii |first5=T |last6=Uchida |first6=K |date=27 May 2016 |title=Identification of lactate dehydrogenase as a mammalian pyrroloquinoline quinone (PQQ)-binding protein. |journal=Scientific Reports |volume=6 |pages=26723 |bibcode=2016NatSR...626723A |doi=10.1038/srep26723 |pmc=4882622 |pmid=27230956}}</ref>

== Controversy regarding role as vitamin ==
The scientific journal ''Nature'' published the 2003 paper by Kasahara and Kato that essentially stated that PQQ was a new vitamin and in 2005, an article by Anthony and Felton that stated that the 2003 Kasahara and Kato paper drew incorrect and unsubstantiated conclusions.<ref>{{Cite journal |vauthors=Felton LM, Anthony C |year=2005 |title=Biochemistry: role of PQQ as a mammalian enzyme cofactor? |journal=Nature |volume=433 |issue=7025 |pages=E10; discussion E11–2 |bibcode=2005Natur.433E..10F |doi=10.1038/nature03322 |pmid=15689995 |s2cid=4370935|doi-access=free }}</ref> An article by ] in ''The Proceedings of the National Academy of Sciences'' in 2018 identified pyrroloquinoline quinone as a "longevity vitamin" not essential for immediate survival, but necessary for long-term health.<ref name="Ames">{{Cite journal |last=Ames |first=Bruce |date=15 October 2018 |title=Prolonging healthy aging: Longevity vitamins and proteins |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=115 |issue=43 |pages=10836–10844 |bibcode=2018PNAS..11510836A |doi=10.1073/pnas.1809045115 |pmc=6205492 |pmid=30322941 |doi-access=free}}</ref>

== See also ==
* ], {{EC number|1.2.1.31}}<ref name="BRENDA PQQ EC1.2.1.31 Homo sapiens">{{Cite encyclopedia |title=L-aminoadipate-semialdehyde dehydrogenase (Homo sapiens) |publisher=Technische Universität Braunschweig |url=http://www.brenda-enzymes.org/enzyme.php?ecno=1.2.1.31&Suchword=&organism%5B%5D=Homo+sapiens&show_tm=0 |access-date=18 July 2015 |date=July 2015 |encyclopedia=BRENDA}}</ref><ref name="PQQ HMDB">{{Cite web |title=Pyrroloquinoline quinone (HMDB13636) |url=http://www.hmdb.ca/metabolites/HMDB13636 |access-date=19 July 2015 |website=Human Metabolome Database |publisher=University of Alberta |postscript=,}} citing:
* {{PMID|2558842}}: "Enzymes containing PQQ are called quinoproteins. PQQ and quinoproteins play a role in the redox metabolism and structural integrity of cells and tissues."
* {{PMID |12712191}}: "It was reported that aminoadipate semialdehyde dehydrogenase (AASDH) might also use PQQ as a cofactor, suggesting a possibility that PQQ is a vitamin in mammals."
</ref>

== References ==
{{Reflist}}

{{Enzyme cofactors}}

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