From Wikipedia, the free encyclopedia
Pyrroloquinoline-quinone synthase
Identifiers
EC no. 1.3.3.11
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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 (1997). "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. S2CID  11735291.


From Wikipedia, the free encyclopedia
Pyrroloquinoline-quinone synthase
Identifiers
EC no. 1.3.3.11
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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 (1997). "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. S2CID  11735291.



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