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Literature summary extracted from
- Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis (2007), Acta Crystallogr. Sect. D, 63, 1059-1068.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.3.44 | expression in Escherichia coli | Pyrococcus horikoshii |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.3.44 | to 2.2 A resolution. The overall structure is a half-barrel structure, composed of six alpha-helices packed against a ten-stranded beta-sheet. Other alpha-helices and two long loops form the walls on both sides of the half-barrel. Construction of a docking model with the FeS clusters, AdoMet and the tRNA | Pyrococcus horikoshii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.3.44 | Pyrococcus horikoshii | O59412 | - |
- |
| 4.1.3.44 | Pyrococcus horikoshii DSM 12428 | O59412 | - |
- |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.3.44 | Fe-S center | residues Cys81, Cys85 and Cys88 are predicted to comprise the iron-sulfur cluster. In the crystal structure, their side chains face each other to create the cluster site | Pyrococcus horikoshii |  |
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Release 2023.1 (January 2023)
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