Warning: mysql_result() [function.mysql-result]: Unable to jump to row 0 on MySQL result index 5 in /net/isilon4/research/thornton/www/databases/html/CSA_NEW/SearchResults.php on line 83
Catalytic Site Atlas Search Results
View the latest EBI news stories and important announcements...

Search The CSA
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1a65

E.C. namelaccase
SpeciesCoprinus cinereus ()
E.C. Number (IntEnz)
CSA Homologues of 1a65There are 55 Homologs
CSA Entries With UniProtID
CSA Entries With EC Number
PDBe Entry 1a65
PDBSum Entry 1a65
MACiE Entry 1a65

Literature Report

IntroductionLaccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water, using three precisely positioned copper ions. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants.
MechansimElectron transport chains around the active site couple the oxidation of various substrates with the reduction of oxygen to water. The most favoured pathway is predicted to start at one copper ion, then go from the sulphur of Cys452 to its carbonyl oxygen, then via a hydrogen bond to the N-delta-1 of His451, which is coordinated to another copper ion.

Catalytic Sites for 1a65

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
CysA452470macie:sideChainPart of the electron transport chain.
CysA452470macie:mainChainCarbonylPart of the electron transport chain.
HisA451469macie:sideChainPart of the electron transport chain.

Literature References

Notes:There may be a second half to the electron transport chain involving Cu903 and the sidechain, carbonyl and amide of His453, but I could not find any evidence of this.
Ferraroni M
Crystallization and preliminary structure analysis of the blue laccase from the ligninolytic fungus Panus tigrinus.
Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 61 205-207
PubMed: 16510995
Piontek K
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
J Biol Chem 2002 277 37663-37669
PubMed: 12163489