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.

Search for more literature for 3.5.1.18

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

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Release 2023.1 (January 2023)