Monofenol monooksigenaza

Monofenol monooksigenaza
Identifikatori
EC broj 1.14.18.1
CAS broj 2594228
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

Monofenol monooksigenaza (EC 1.14.18.1, fenolaza, monofenol oksidaza, krezolaza, monofenolaza, tirozin-dopa oksidaza, monofenolna monooksidaza, monofenol dihidroksifenilalanin:kiseonik oksidoreduktaza, N-acetil-6-hidroksitriptofan oksidaza, monofenol, dihidroksi-L-fenilalanin kiseonik oksidoreduktaza, o-difenol:O2 oksidoreduktaza, fenol oksidaza) je enzim sa sistematskim imenom L-tirozin,L-dopa:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10][11][12] Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) L-tirozin + O2 ⇌ {\displaystyle \rightleftharpoons } dopahinon + H2O (sveukupna reakcija)
(1a) L-tirozin + 1/2 O2 ⇌ {\displaystyle \rightleftharpoons } L-dopa
(1b) L-dopa + 1/2 O2 ⇌ {\displaystyle \rightleftharpoons } dopahinon +H2O
(2) 2 L-dopa + O2 ⇌ {\displaystyle \rightleftharpoons } 2 dopahinon + 2H2O

Ovaj enzim je tip III bakarni protein prisutan u širokom varijetetu bakterija, gljiva, biljki, insekata, rakova i sisara. On učestvuje u sintezi betalaina i melanina.

Reference

  1. ↑ Dawson, C.R. and Tarpley, W.B. (1951). „The copper oxidases”. u: Sumner, J.B. and Myrbäck, K.. The Enzymes. 2 (1st izd.). New York: Academic Press. str. 454-498. 
  2. ↑ Patil, S.S. and Zucker, M. (1965). „Potato phenolases. Purification and properties”. J. Biol. Chem. 240: 3938-3943. PMID 5842066. 
  3. ↑ Pomerantz, S.H. (1963). „Separation, purification, and properties of two tyrosinases from hamster melanoma”. J. Biol. Chem. 238: 2351-2357. PMID 13972077. 
  4. ↑ Pomerantz, S.H. (1963). „Separation, purification, and properties of two tyrosinases from hamster melanoma”. J. Biol. Chem. 238: 2351-2357. PMID 13972077. 
  5. ↑ Robb, D.A. (1984). „`Tyrosinase”. u: Lontie, R.. Copper Proteins and Copper Enzymes. 2. Boca Raton, FL: CRC Press. str. 207-240. 
  6. ↑ Robb, D.A. (1984). „`Tyrosinase”. u: Lontie, R.. Copper Proteins and Copper Enzymes. 2. Boca Raton, FL: CRC Press. str. 207-240. 
  7. ↑ Sanchez-Ferrer, A., Rodriguez-Lopez, J.N., Garcia-Canovas, F. and Garcia-Carmona, F. (1995). „Tyrosinase: a comprehensive review of its mechanism”. Biochim. Biophys. Acta 1247: 1-11. PMID 7873577. 
  8. ↑ Sanchez-Ferrer, A., Rodriguez-Lopez, J.N., Garcia-Canovas, F. and Garcia-Carmona, F. (1995). „Tyrosinase: a comprehensive review of its mechanism”. Biochim. Biophys. Acta 1247: 1-11. PMID 7873577. 
  9. ↑ Steiner, U., Schliemann, W. and Strack, D. (1996). „Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures”. Anal. Biochem. 238: 72-75. PMID 8660589. 
  10. ↑ Steiner, U., Schliemann, W. and Strack, D. (1996). „Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures”. Anal. Biochem. 238: 72-75. PMID 8660589. 
  11. ↑ Rolff, M., Schottenheim, J., Decker, H. and Tuczek, F. (2011). „Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme”. Chem Soc Rev 40: 4077-4098. PMID 21416076. 
  12. ↑ Rolff, M., Schottenheim, J., Decker, H. and Tuczek, F. (2011). „Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme”. Chem Soc Rev 40: 4077-4098. PMID 21416076. 

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. 
  • Robb, D.A. (1984). „`Tyrosinase”. u: Lontie, R.. Copper Proteins and Copper Enzymes. 2. Boca Raton, FL: CRC Press. str. 207-240. 
  • Robb, D.A. (1984). „`Tyrosinase”. u: Lontie, R.. Copper Proteins and Copper Enzymes. 2. Boca Raton, FL: CRC Press. str. 207-240. 
  • Dawson, C.R. and Tarpley, W.B. (1951). „The copper oxidases”. u: Sumner, J.B. and Myrbäck, K.. The Enzymes. 2 (1st izd.). New York: Academic Press. str. 454-498. 

Spoljašnje veze

  • 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