Literature summary extracted from
Crutcher, F.K.; Moran-Diez, M.E.; Krieger, I.V.; Kenerley, C.M.
Effects on hyphal morphology and development by the putative copper radical oxidase glx1 in Trichoderma virens suggest a novel role as a cell wall associated enzyme (2019), Fungal Genet. Biol., 131, 103245 .
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.2.3.15 |
Cu2+ |
enzyme is a copper radical oxidase. Residues comprising the copper coordinating active site and the radical redox site are Cys228, Tyr272, Tyr495, His496, and His581 |
Trichoderma virens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.3.15 |
Trichoderma virens |
- |
- |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.2.3.15 |
? |
x * 77000, SDS-PAGE |
Trichoderma virens |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.2.3.15 |
Glx1 |
- |
Trichoderma virens |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.2.3.15 |
physiological function |
silencing of the glx1 gene results in mutants with more than 90% expression reduction and the absence of glyoxal oxidase catalytic activity. The mutants show delayed hyphal growth, reduced colony and conidial hydrophobicity, but no changes in their biocontrol ability. Mutants exhibit a loss of growth directionality resulting in a curled phenotype that is eliminated in the presence of exogenous H2O2 |
Trichoderma virens |