EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.16 | to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state | Arabidopsis thaliana |
2.3.1.16 | to 1.8 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state | Helianthus annuus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.16 | cystamine | 10 mM, inactivation with half-life of 0.6 h | Arabidopsis thaliana | |
2.3.1.16 | additional information | in presence of 20 mM cysteamine, full activity is maintained for more than 12 h | Arabidopsis thaliana |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.1.16 | peroxisome | - |
Arabidopsis thaliana | 5777 | - |
2.3.1.16 | peroxisome | - |
Helianthus annuus | 5777 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.16 | Arabidopsis thaliana | Q56WD9 | - |
- |
2.3.1.16 | Helianthus annuus | Q6W6X6 | - |
- |
EC Number | Storage Stability | Organism |
---|---|---|
2.3.1.16 | in the absence of both cystamine and cysteamine isoform KAT2 spontaneously inactivates with a half-life | Arabidopsis thaliana |
2.3.1.16 | of 2.6 h | Arabidopsis thaliana |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.16 | More | enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling | Arabidopsis thaliana |
2.3.1.16 | More | enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling | Helianthus annuus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.16 | KAT2 | - |
Arabidopsis thaliana |
2.3.1.16 | KAT2 | - |
Helianthus annuus |