Pirolohinolin-hinon sintaza

Pirolohinolin-hinon sintaza
Identifikatori
EC broj 1.3.3.11
CAS broj 353484-42-1
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

Pirolohinolin-hinon sintaza (EC 1.3.3.11, PqqC, 6-(2-amino-2-karboksietil)-7,8-diokso-1,2,3,4,5,6,7,8-oktahidrohinolin-2,4-dikarboksilat:kiseonik oksidoreduktaza (ciklizacija)) je enzim sa sistematskim imenom 6-(2-amino-2-karboksietil)-7,8-diokso-1,2,3,4,7,8-heksahidrohinolin-2,4-dikarboksilat:kiseonik oksidoreduktaza (ciklizacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

6-(2-amino-2-karboksietil)-7,8-diokso-1,2,3,4,7,8-heksahidrohinolin-2,4-dikarboksilat + 3 O2 {\displaystyle \rightleftharpoons } 4,5-diokso-4,5-dihidro-1H-pirolo[2,3-f]hinolin-2,7,9-trikarboksilat + 2H2O2 + 2H2O

Za rad ovog enzima je neophodna jedna za sad neophodna komponenta da bi došlo do oslobađanja njegovog produkta.

Reference

  1. Magnusson, O.T., Toyama, H., Saeki, M., Schwarzenbacher, R. and Klinman, J.P. (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: 5342-5343. PMID 15113189. 
  2. Magnusson, O.T., Toyama, H., Saeki, M., Rojas, A., Reed, J.C., Liddington, R.C., Klinman, J.P. and Schwarzenbacher, R. (2004). „Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone”. Proc. Natl. Acad. Sci. USA 101: 7913-7918. PMID 15148379. 
  3. Toyama, H., Chistoserdova, L. and Lidstrom, M.E. (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: 595-602. PMID 9043136. 
  4. Toyama, H., Fukumoto, H., Saeki, M., Matsushita, K., Adachi, O. and Lidstrom, M.E. (2002). „PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone”. Biochem. Biophys. Res. Commun. 299: 268-272. PMID 1243798. 
  5. Schwarzenbacher, R., Stenner-Liewen, F., Liewen, H., Reed, J.C. and Liddington, R.C. (2004). „Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 A resolution”. Proteins 56: 401-403. PMID 15211525. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • MeSH Pyrroloquinoline-quinone+synthase
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6