Any feedback?
Literature summary for 2.5.1.46 extracted from
- Trypanosomatid deoxyhypusine synthase activity is dependent on shared active-site complementation between pseudoenzyme paralogs (2018), Structure, 26, 1499-1512 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Trypanosoma brucei brucei |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| heterotetramer, to 3.5 A resolution. The activity is dependent on heterotetramer formation between paralogs DHSc and DHSp. The X-ray structure of DHS shows a single functional shared active site formed at the DHSc/DHSp heterodimer interface. Deficiencies in one subunit are complemented by the other | Trypanosoma brucei brucei |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D218A | mutation in catalytic site of subunit DHSp, mutant is unable to catalyze the single-turnover formation of NADH | Trypanosoma brucei brucei |
| D405A | mutation in catalytic site of subunit DHSc, impaired in activity | Trypanosoma brucei brucei |
| E103A | mutation in catalytic site of subunit DHSp, impaired in activity | Trypanosoma brucei brucei |
| E104A | mutation in catalytic site of subunit DHSp, impaired in activity | Trypanosoma brucei brucei |
| E166A | mutation in dead site of subunit DHSc, activity is similar to wild-type. The heterotetrameric complex shows a decrease in melting temperature by 4.9 degrees | Trypanosoma brucei brucei |
| H266A | mutation in dead site of subunit DHSp, activity is similar to wild-type | Trypanosoma brucei brucei |
| additional information | mutation of sets of matched pairs, where the same residue is changed in both the catalytic and dead site, melting temperature of mutants is similar to wild-type | Trypanosoma brucei brucei |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0012 | - |
NAD+ | mutant E166A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei |  |
| 0.0013 | - |
NAD+ | wild-type, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.0098 | - |
spermidine | wild-type, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.011 | - |
spermidine | mutant E166A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.012 | - |
spermidine | mutant H266A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.098 | - |
NAD+ | mutant H266A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma brucei brucei | Q38BX0 and Q4GZD1 | Q38BX0 i.e. catalytic subunit DHSc, Q4GZD1 i.e. regulatory subunit DHSp | - |
| Trypanosoma brucei brucei 927/4 GUTat10.1 | Q38BX0 and Q4GZD1 | Q38BX0 i.e. catalytic subunit DHSc, Q4GZD1 i.e. regulatory subunit DHSp | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| spermidine + NAD+ | - |
Trypanosoma brucei brucei | dehydrospermidine + NADH | - |
? | |
| spermidine + NAD+ | - |
Trypanosoma brucei brucei 927/4 GUTat10.1 | dehydrospermidine + NADH | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DHSc | - |
Trypanosoma brucei brucei |
| DHSp | - |
Trypanosoma brucei brucei |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 56 | - |
melting temperature, wild-type | Trypanosoma brucei brucei |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.081 | - |
spermidine | mutant H266A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.12 | - |
spermidine | mutant E166A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.15 | - |
NAD+ | wild-type, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.16 | - |
NAD+ | mutant E166A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.16 | - |
NAD+ | mutant H266A, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
| 0.18 | - |
spermidine | wild-type, pH not specified in the publication, temperature not specified in the publication | Trypanosoma brucei brucei | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | each enzyme heterodimer contains two NAD+ binding sites, one housed in the functional catalytic site and the second bound in a remnant dead site that lacks key catalytic residues | Trypanosoma brucei brucei | |
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
