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The tridimensional structure of this enzyme has not been resolved yet.
N-acetylornithinase
5.Acting on carbon-nitrogen bonds, other than peptide bonds
1.In linear amides
acetate
+ L-ornithinaH2O
N-acetyl-methionine
L-ornithina
L-methionine
Also hydrolyzes N-acetylmethionine.
Belongs to a family of enzymes that share a few characteristics. They hydrolyse peptidic bonds in substrates that share a common structure, they are dependent on cobalt or zinc for their activity and they are proteins of 40 Kd to 60 Kd with a number of regions of sequence similarity. As signature patterns for these proteins, it has been selected two of the conserved regions. The first pattern contains a conserved histidine which could be involved in binding metal ions and the second pattern contains a number of conserved charged residues. Also belongs to the family yhe enzyme succinyl
diaminopimetale desuccinylase (EC 3.5.1.18).
Reference