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Literature summary for 3.5.1.16 extracted from
- Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase (2000), Biochemistry, 39, 1285-1293.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | - |
Escherichia coli |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| PCR-amplified argE, cloned and expressed | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,10-phenanthroline | zinc-specific chelator | Escherichia coli | |
| acetate | product inhibition | Escherichia coli | |
| EDTA | - |
Escherichia coli | |
| NaF | linear uncompetitive inhibition | Escherichia coli | |
| ornithine | product inhibition | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.81 | - |
Nalpha-acetyl-L-methionine | - |
Escherichia coli | |
| 1 | - |
Nalpha-acetyl-L-alanine | - |
Escherichia coli | |
| 1.3 | - |
Nalpha-Acetyl-L-ornithine | in presence of Co2+ or Ni2+ | Escherichia coli | |
| 2 | - |
N-formyl-L-methionine | - |
Escherichia coli | |
| 2.2 | - |
acetylornithine | in presence of Mg2+ | Escherichia coli | |
| 2.4 | - |
Nalpha-acetyl-L-glutamine | - |
Escherichia coli | |
| 2.5 | - |
Nalpha-Acetyl-L-ornithine | - |
Escherichia coli | |
| 3.8 | - |
Nalpha-Acetyl-L-ornithine | in presence of Cd2+ | Escherichia coli | |
| 4.1 | - |
Nalpha-acetyl-L-lysine | - |
Escherichia coli | |
| 6.7 | - |
Nalpha-acetyl-DL-serine | - |
Escherichia coli | |
| 7 | - |
Nalpha-acetyl-L-leucine | - |
Escherichia coli | |
| 7 | - |
Nalpha-chloroacetylglycine | - |
Escherichia coli | |
| 7.2 | - |
Nalpha-Acetyl-L-ornithine | in presence of Zn2+ | Escherichia coli | |
| 8.3 | - |
Nalpha-acetyl-L-asparagine | - |
Escherichia coli | |
| 13 | - |
Nalpha-acetyl-L-cysteine | - |
Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | enzyme is a metalloprotein, activated by a Co2+ complex | Escherichia coli | |
| Co2+ | activity increases 8fold | Escherichia coli | |
| PO43- | activation | Escherichia coli | |
| Zn2+ | 0.1 mM activity increases 2-fold, further increase in concentration results in inhibition | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42350 | - |
deduced from nucleotide sequence of argE gene | Escherichia coli |
| 42350 | - |
electrospray ionization mass spectrometry | Escherichia coli |
| 43000 | - |
- |
Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N2-acety-L-ornithine + H2O | Escherichia coli | step in arginine biosynthesis | L-ornithine + acetate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
K-12 | - |
| Escherichia coli | - |
160-37 | - |
| Escherichia coli | - |
ATCC9637 | - |
| Escherichia coli 160-37 | - |
160-37 | - |
| Escherichia coli ATCC 9637 | - |
ATCC9637 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of recombinant enzyme | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acetyl-DL-methionine + H2O | - |
Escherichia coli | methionine + acetate | - |
? | |
| N-acetyl-DL-methionine + H2O | - |
Escherichia coli 160-37 | methionine + acetate | - |
? | |
| N-acetyl-DL-methionine + H2O | - |
Escherichia coli ATCC 9637 | methionine + acetate | - |
? | |
| N-formyl-L-methionine + H2O | - |
Escherichia coli | L-methionine + formate | - |
? | |
| N-formyl-L-methionine + H2O | - |
Escherichia coli 160-37 | L-methionine + formate | - |
? | |
| N-formyl-L-methionine + H2O | - |
Escherichia coli ATCC 9637 | L-methionine + formate | - |
? | |
| N2-acety-L-ornithine + H2O | step in arginine biosynthesis | Escherichia coli | L-ornithine + acetate | - |
? | |
| Nalpha-acetyl-DL-serine + H2O | - |
Escherichia coli | DL-serine + acetate | - |
? | |
| Nalpha-acetyl-L-alanine + H2O | - |
Escherichia coli | L-alanine + acetate | - |
? | |
| Nalpha-acetyl-L-alanine + H2O | - |
Escherichia coli 160-37 | L-alanine + acetate | - |
? | |
| Nalpha-acetyl-L-alanine + H2O | - |
Escherichia coli ATCC 9637 | L-alanine + acetate | - |
? | |
| Nalpha-acetyl-L-asparagine + H2O | - |
Escherichia coli | L-asparagine + acetate | - |
? | |
| Nalpha-acetyl-L-cysteine + H2O | - |
Escherichia coli | L-cysteine + acetate | - |
? | |
| Nalpha-acetyl-L-glutamine + H2O | - |
Escherichia coli | L-glutamine + acetate | - |
? | |
| Nalpha-acetyl-L-glutamine + H2O | - |
Escherichia coli 160-37 | L-glutamine + acetate | - |
? | |
| Nalpha-acetyl-L-glutamine + H2O | - |
Escherichia coli ATCC 9637 | L-glutamine + acetate | - |
? | |
| Nalpha-acetyl-L-leucine + H2O | - |
Escherichia coli | L-leucine + acetate | - |
? | |
| Nalpha-acetyl-L-lysine + H2O | - |
Escherichia coli | L-lysine + acetate | - |
? | |
| Nalpha-acetyl-L-methionine + H2O | - |
Escherichia coli | acetate + L-methionine | - |
? | |
| Nalpha-acetyl-L-ornithine + H2O | - |
Escherichia coli | L-ornithine + acetate | - |
? | |
| Nalpha-acetyl-L-ornithine + H2O | - |
Escherichia coli 160-37 | L-ornithine + acetate | - |
? | |
| Nalpha-acetyl-L-ornithine + H2O | - |
Escherichia coli ATCC 9637 | L-ornithine + acetate | - |
? | |
| Nalpha-chloroacetylglycine + H2O | - |
Escherichia coli | glycine + chloroacetate | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.3 | 8.7 | - |
Escherichia coli |
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