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Literature summary for 3.5.1.28 extracted from
- Amidase activity is essential for medial localization of AmiC in Caulobacter crescentus (2018), Curr. Genet., 64, 661-675 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genen amiC, functional recombinant expression in Escherichia coli, enzyme AmiC complements and restores cell separation defects seen in Escherichia coli amidase mutants | Caulobacter vibrioides |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E196A | site-directed mutagenesis, active site mutant | Caulobacter vibrioides |
| H182A | site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview | Caulobacter vibrioides |
| H250A | site-directed mutagenesis, active site mutant | Caulobacter vibrioides |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the enzyme belongs to the divisome. AmiC recruitment to divisome is independent of endopeptidase DipM | Caulobacter vibrioides | 16020 | - |
| additional information | the amidase-3 family catalytic domain of AmiC is essential for medial localization | Caulobacter vibrioides | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Caulobacter vibrioides | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | ? | - |
? |  |
| additional information | Caulobacter vibrioides CB15N | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | ? | - |
? | |
| additional information | Caulobacter vibrioides NA1000 | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Caulobacter vibrioides | A0A0H3C9I3 | - |
- |
| Caulobacter vibrioides CB15N | A0A0H3C9I3 | - |
- |
| Caulobacter vibrioides NA1000 | A0A0H3C9I3 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | Caulobacter vibrioides | ? | - |
? | |
| additional information | enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan | Caulobacter vibrioides | ? | - |
? | |
| additional information | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | Caulobacter vibrioides CB15N | ? | - |
? | |
| additional information | enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan | Caulobacter vibrioides CB15N | ? | - |
? | |
| additional information | in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC | Caulobacter vibrioides NA1000 | ? | - |
? | |
| additional information | enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan | Caulobacter vibrioides NA1000 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmiC | - |
Caulobacter vibrioides |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Caulobacter vibrioides |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Caulobacter vibrioides |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | overexpression of AmiC causes cell separation defects and formation of chains, and overexpression of AmiC in cells inhibited for cell division leads to lysis. Overexpression of amidase leads to morphological aberrations | Caulobacter vibrioides |
| metabolism | analysis of regulation of daughter cell separation in Caulobacter crescentus, comparison with Escherichia coli | Caulobacter vibrioides |
| physiological function | enzyme AmiC has septum splitting activity and can perform septal peptidoglycan splitting, it probably plays a role in cell separation. The enzymatic activity is essential for medial recruitment of AmiC, the amidase-3 family catalytic domain of AmiC is essential for medial localization. AmiC is a late cell division protein, overview | Caulobacter vibrioides |
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