Any feedback?
Literature summary for 2.3.1.12 extracted from
- Mapping the lipoylation site of Arabidopsis thaliana plastidial dihydrolipoamide S-acetyltransferase using mass spectrometry and site-directed mutagenesis (2011), Plant Physiol. Biochem., 49, 1355-1361.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K96A | mutation in potential lipoylation site, mutant protein entirely supports the assignment of Lys96 as the site of lipoylation | Arabidopsis thaliana |
| K96R | mutation in potential lipoylation site, mutant protein entirely supports the assignment of Lys96 as the site of lipoylation | Arabidopsis thaliana |
| additional information | protein includes a single lipoyl-prosthetic group covalently attached to Lys96. Despite low primary sequence identity with the bacterial enzyme, the plant protein is recognized and modified by Escherichia coli E2 lipoyl-addition system | Arabidopsis thaliana |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plastid | - |
Arabidopsis thaliana | 9536 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 59000 | - |
x * 59000, SDS-PAGE, recombinant protein | Arabidopsis thaliana |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 59000, SDS-PAGE, recombinant protein | Arabidopsis thaliana |
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
