Pyrroloquinoline-quinone synthase

Identifiers

EC number

1.3.3.11

Databases

PDB structures

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In enzymology, a pyrroloquinoline-quinone synthase (EC 1.3.3.11) is an enzyme that catalyzes the chemical reaction

6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O₂

\rightleftharpoons

4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline- 2,7,9-tricarboxylate + 2 H₂O₂ + 2 H₂O

The two substrates of this enzyme are 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate, and O₂, whereas its 3 products are 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, H₂O₂, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinol ine-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing). This enzyme is also called PqqC.

References

Magnusson OT, Toyama H, Saeki M, Schwarzenbacher R, Klinman JP (2004). "The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis". J. Am. Chem. Soc. 126 (17): 5342–3. doi:10.1021/ja0493852. PMID 15113189.
Klinman JP, Schwarzenbacher R (2004). "Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone". Proc. Natl. Acad. Sci. U.S.A. 101 (21): 7913–8. doi:10.1073/pnas.0402640101. PMC 419531. PMID 15148379.
Toyama H, Chistoserdova L, Lidstrom ME. "Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate". Microbiology. 143 (2): 595–602. doi:10.1099/00221287-143-2-595. PMID 9043136.
Yasunaga K (1975). "[Concept of thrombocytopathy and problems involved in its diagnosis (author's transl)]". Nippon. Ketsueki. Gakkai. Zasshi. 38 (6): 734–40. PMID 1243798.
RC; Stenner-Liewen, F; Liewen, H; Reed, JC; Liddington, RC (2004). "Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 A resolution". Proteins. 56 (2): 401–3. doi:10.1002/prot.20085. PMID 15211525.

Oxidoreductases: CH–CH oxidoreductases (EC 1.3)

1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase

1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase

1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD

1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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