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Literature summary for 2.3.1.117 extracted from
- The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism (2009), J. Mol. Biol., 389, 863-879.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E199A | completely inactive mutant | Mycobacterium tuberculosis |
| G222P | completely inactive mutant | Mycobacterium tuberculosis |
| additional information | binary complex of Mtb-DapD and succinyl-CoA | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acetate | caused by inhibition of succinyl-CoA-binding or pH effect | Mycobacterium tuberculosis |  |
| Co2+ | partial inhibition | Mycobacterium tuberculosis | |
| Zn2+ | 1 mM, complete loss of enzyme acitivity | Mycobacterium tuberculosis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | slight increase of enzyme activity | Mycobacterium tuberculosis | |
| Mg2+ | stabilizes quartenary enzyme structure, slight increase of enzyme activity | Mycobacterium tuberculosis | |
| Mn2+ | slight increase of enzyme activity | Mycobacterium tuberculosis | |
| Na+ | stabilizes quartenary enzyme structure | Mycobacterium tuberculosis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WP21 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| affinity and size-exclusion chromatography | Mycobacterium tuberculosis |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | - |
Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DapD | - |
Mycobacterium tuberculosis |
| Mtb-DapD | in complex with cofactor succinyl-CoA | Mycobacterium tuberculosis |
| tetrahydrodipicolinate N-succinyltransferase | - |
Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | part of L-lysine biosynthetic pathway | Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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