amidase

The specific reaction catalyzed the amidase genes is not predicted.

These three residues also block the catalytic Cys-59 in the amidase domain.

Other names in common use include N-acylethanolamine amidohydrolase, and acylethanolamine amidase.

This enzyme is also called carbamoylsarcosine amidase.

The N-terminal domain is a cysteine, histidine-dependent aminohydrolase amidase.

Inhibition of isoniazid-induced hepatotoxicity in rabbits by pretreatment with an amidase inhibitor.

This low activity can be explained by the blocking of the catalytic Cys in the amidase active site in order for the protein to properly fold.

N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.

Peptide amidase (Pam), which catalyses the hydrolysis of the C-terminal amide bond of peptides.

It produces penicillin amidase used to make synthetic penicillin, various amylases used in the baking industry and glucose dehydrogenase used in glucose blood tests.

An additional domain is found at the N-terminal of some copper amine oxidases, as well as in related proteins such as cell wall hydrolase and N-acetylmuramoyl-L-alanine amidase.

The CHAP domain is found in a wide range of protein architectures; it is commonly associated with bacterial type SH3 domains and with several families of amidase domains.

A third subfamily of the AcmB/LytN-like family is typified by the amino-terminal amidase domain of the GSPS from γ-proteobacteria and trypanosomes [ 26, 55, 56].

Partial synteny of the αr45 genomic regions was observed in the Mesorhizobium and Brucella species where instead of aLysR family transcriptional regulator' gene an amidase coding gene was found.

Under conditions found to be the optimum for both the forward and backwards reactions, trypanothione synthase from trypanosoma cruzi was found to have an amidase activity that was only about 1% of the forwards synthetase activity.

It is found in the potential 5' untranslated regions (5' UTRs) of livK genes and downstream livM and livH genes, as well as the 5' UTRs of amidase genes.

Thus, these proteins contain fusions of the NlpC/P60 peptidase domain with the SH3, choline-binding, LysM, lysozyme and NAM amidase domains (Figure 4), and this implicates them in different processes in cell-wall dynamics.

PEA is metabolized by cellular enzymes, fatty acid amide hydrolase (FAAH) and N-acylethanolamine-hydrolyzing acid amidase (NAAA), the latter of which has more specificity toward PEA over other fatty acid amides.

Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid, consequently it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity.

Endopeptidase lysins cleave any of the peptide bonds between amino acids, whereas N-acetylmuramoyl-l-alanine amidase lysins (or simply amidase lysins) hydrolyze the amide bond between the sugar and the amino acid moieties.