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Literature summary for 3.5.1.18 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

Cloned(Commentary)

Cloned (Comment) Organism
gene dapE, sequence comparison Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure, PDB ID 3IC1, analysis, comparison with the structure of N-acetyl-L-ornithine deacetylase, EC 3.5.1.16, overview Haemophilus influenzae

Metals/Ions

Metals/Ions Comment Organism Structure
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 0.0044 mM, whereas the observed Kd values for the second metal binding event in DapE is 0.0136 mM Haemophilus influenzae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-succinyl-LL-2,6-diaminoheptanedioate + H2O Haemophilus influenzae
-
succinate + LL-2,6-diaminoheptanedioate
-
?

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
gene dapE
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-LL-2,6-diaminoheptanedioate + H2O
-
Haemophilus influenzae succinate + LL-2,6-diaminoheptanedioate
-
?

Synonyms

Synonyms Comment Organism
DapE
-
Haemophilus influenzae
N-succinyl-L,L-diaminopimelic acid desuccinylase
-
Haemophilus influenzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Haemophilus influenzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Haemophilus influenzae

General Information

General Information Comment Organism
additional information DapE residues H355 and H80 are active site ligands, divalent metal binding properties of co-catalytic metallohydrolase active site, overview. Three-dimensional homological structure molecular modeling of N-acetyl-L-ornithine deacetylase, EC 3.5.1.16, from Escherichia coli, using the X-ray crystal structure of the DapE from Haemophilus influenzae, PDB ID 3IC1, as template Haemophilus influenzae