Any feedback?
Literature summary for 5.3.1.5 extracted from
- Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex (1995), Biochemistry, 34, 3742-3749.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| D-threonohydroxamic acid soaked into the crystal, crystallographic structure at 1.6 A resolution | Streptomyces olivochromogenes |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| D-Threonohydroxamic acid | slow-binding competitive inhibitor with glucose as substrate | Streptomyces olivochromogenes |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces olivochromogenes | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Xylose | - |
Streptomyces olivochromogenes | D-Xylulose | - |
? | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
