Laccase

Laccase
Identifiers
EC no.1.10.3.2
CAS no.80498-15-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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Laccases (EC 1.10.3.2) are multicopper oxidases found in plants, fungi, and bacteria. Laccases oxidize a variety of phenolic substrates, performing one-electron oxidations, leading to crosslinking. For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols.[1] Other laccases, such as those produced by the fungus Pleurotus ostreatus, play a role in the degradation of lignin, and can therefore be classed as lignin-modifying enzymes.[2] Other laccases produced by fungi can facilitate the biosynthesis of melanin pigments.[3] Laccases catalyze ring cleavage of aromatic compounds.[4]

Laccase was first studied by Hikorokuro Yoshida in 1883 and then by Gabriel Bertrand[5] in 1894[6] in the sap of the Japanese lacquer tree, where it helps to form lacquer, hence the name laccase.

  1. ^ Solomon EI, Sundaram UM, Machonkin TE (November 1996). "Multicopper Oxidases and Oxygenases". Chemical Reviews. 96 (7): 2563–2606. doi:10.1021/cr950046o. PMID 11848837.
  2. ^ Cite error: The named reference cohen02 was invoked but never defined (see the help page).
  3. ^ Cite error: The named reference Lee D was invoked but never defined (see the help page).
  4. ^ Claus H (2004). "Laccases: structure, reactions, distribution". Micron. 35 (1–2): 93–96. doi:10.1016/j.micron.2003.10.029. PMID 15036303.
  5. ^ "Gabriel Bertrand on isimabomba" (in French).
  6. ^ Lu GD, Ho PY, Sivin N (1980-09-25). Science and civilisation in China: Chemistry and chemical. Vol. 5. Cambridge University Press. p. 209. ISBN 9780521085731.