amidohydrolase

The systematic name of this enzyme class is L-5-carboxymethylhydantoin amidohydrolase.

Other names in common use include 4-methyleneglutamine deamidase, and 4-methyleneglutamine amidohydrolase.

This enzyme is also called allantoate amidohydrolase.

Its systemic name is barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming).

Although grouped into the naturally existing amidohydrolases, it demonstrates more homology with cyanuric acid amidohydrolase.

Other names in common use include imidase, cyclic imide hydrolase, and cyclic-imide amidohydrolase (decyclicizing) [misprint].

Protein N-terminal glutamine amidohydrolase is an enzyme that in humans is encoded by the WDYHV1 gene.

This enzyme belongs to the Amidohydrolase superfamily of enzymes and is a member of Cluster of Orthologous Groups (COG) 3618.

These predictions are then tested by five Bridging Projects representing the amidohydrolase, enolase, GST, HAD, and isoprenoid synthase enzyme superfamilies.

LigI from Sphingomonas is of particular interest as it has been shown to be the first member of the amidohydrolase superfamily to not require a divalent metal cation for catalytic activity.

The amidohydrolase superfamily contains evolutionarily related enzymes with a distorted (β/α)8 barrel fold which primarily catalyze metal-assisted deamination, decarboxylation, isomerization, hydration, or retroaldol cleavage reactions.

However, the fact that CRMPs are not enzymatic reveals that they might lack the critical His residues that are present in amidohydrolase enzymes to allow them to bind metal atoms to their active site.

Neutral ceramidase C also known as N-acylsphingosine amidohydrolase 2C or non-lysosomal ceramidase C or ASAH2C is a ceramidase enzyme which in humans is encoded by the ASAH2C gene.

Other names in common use include benzyloxycarbonylglycine hydrolase, Nalpha-carbobenzoxyamino acid amidohydrolase, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase, and Nalpha-benzyloxycarbonyl amino acid urethane hydrolase I. It has 2 cofactors: zinc, and Cobalt.

First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of adenosylcobinamide-phosphate synthase (CbiB).