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Literature summary for 4.4.1.3 extracted from
- New mechanistic insight from substrate- and product-bound structures of the metal-dependent dimethylsulfoniopropionate lyase DddQ (2016), Biochemistry, 55, 6162-6174 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with Fe(III) and substrate dimethylsulfoniopropionate, to 2.0-2.5 A resolution. The enzyme undergoes conformational changes upon substrate-binding. The substrate is positioned optimally to bind iron and is in the proximity of Tyr120 that acts as a Lewis base to initiate catalysis | Ruegeria lacuscaerulensis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | isolated protein contains 0.5 Fe per subunit. The UV-visible spectrum exhibits a feature at 550 nm, consistent with a tyrosinate-Fe(III) ligand-to-metal charge transfer transition. Both the Fe(III) oxidized and Fe(II) reduced species are active | Ruegeria lacuscaerulensis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ruegeria lacuscaerulensis | D0CY60 | - |
- |
| Ruegeria lacuscaerulensis DSM 11314 | D0CY60 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Ruegeria lacuscaerulensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DddQ | - |
Ruegeria lacuscaerulensis |
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