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Literature summary for 3.5.1.16 extracted from

  • McGregor, W.C.; Gillner, D.M.; Swierczek, S.I.; Liu, D.; Holz, R.C.
    Identification of a histidine metal ligand in the argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli (2013), SpringerPlus, 2, 482.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene argE, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21, wild-type and mutant H355A are soluble, the other mutants are insoluble Escherichia coli

Protein Variants

Protein Variants Comment Organism
H355A site-directed mutagenesis, the mutation affects a key aspect of the active site of the enzyme, i.e. metal cofactor binding. The mutant contains no Zn2+ ions but requires Zn2+ for activity, decrease in activity of H355A due to a 380fold decrease in kcat. The catalytic efficiency for the Co(II)-loaded H355A mutant enzyme is about 160fold less than the Co(II)-loaded wild-type enzyme Escherichia coli
H355K site-directed mutagenesis Escherichia coli
H80A site-directed mutagenesis Escherichia coli
H80K site-directed mutagenesis Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can substitute for Zn2+ Escherichia coli
Zn2+ required, the enzyme binds two Zn(II) ions in non-interactive binding sites with Kd values for the first Zn(II) binding event of 0.0027 mM, whereas the observed Kd values for the second metal binding event in DapE is 0.051 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene argE
-

Renatured (Commentary)

Renatured (Comment) Organism
refolding of mutants H355K, H80A, and H80K from inclusion bodies after recombinant expression in Escherichia coli strain BL21 is not sucessfull Escherichia coli

Synonyms

Synonyms Comment Organism
ArgE
-
 Escherichia coli
N-acetyl-L-ornithine deacetylase
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
additional information three-dimensional homologic structure, molecular modeling using the X-ray crystal structure of the DapE from Haemophilus influenzae, PDB ID 3IC1, as template, overview Escherichia coli