GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:22389745
| Citation |
Preeti, , Tapas, S, Kumar, P, Madhubala, R and Tomar, S (2012) Biochemical, mutational and in silico structural evidence for a functional dimeric form of the ornithine decarboxylase from Entamoeba histolytica. PLoS Negl Trop Dis 6:e1559 |
|---|---|
| Abstract |
Entamoeba histolytica is responsible for causing amoebiasis. Polyamine biosynthesis pathway enzymes are potential drug targets in parasitic protozoan diseases. The first and rate-limiting step of this pathway is catalyzed by ornithine decarboxylase (ODC). ODC enzyme functions as an obligate dimer. However, partially purified ODC from E. histolytica (EhODC) is reported to exist in a pentameric state. |
| Links |
PubMed PMC3289617 Online version:10.1371/journal.pntd.0001559 |
| Keywords |
Amino Acid Substitution; Catalytic Domain; Chromatography, Gel; Circular Dichroism; Entamoeba histolytica/enzymology; Entamoeba histolytica/genetics; Enzyme Stability; Escherichia coli/genetics; Mass Spectrometry; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Mutant Proteins/chemistry; Mutant Proteins/genetics; Mutant Proteins/isolation & purification; Mutant Proteins/metabolism; Ornithine Decarboxylase/chemistry; Ornithine Decarboxylase/genetics; Ornithine Decarboxylase/isolation & purification; Ornithine Decarboxylase/metabolism; Protein Conformation; Protein Multimerization; Protein Stability; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004586: ornithine decarboxylase activity |
ECO:0000315: |
F |
Fig. 10: the four ODC mutants show significantly reduced enzyme activity compared to the wild type ODC. |
complete | ||||
|
enables |
GO:0004586: ornithine decarboxylase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
See Help:References for how to manage references in GONUTS.
