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Literature summary for 1.2.3.15 extracted from
- 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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trichoderma virens | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 77000, SDS-PAGE | Trichoderma virens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Glx1 | - |
Trichoderma virens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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