Amidase

  1. Kelompok enzim yang mengkatalisis pemecahan ikatan karbon-nitrogen pada amida.
  2. Enzim yang mengkatalisis pemacahan ikatan karbon-nitrogen pada amida asam monokarboksilat menjadi bentuk asam monokarboksilat dan amonia.
Merriam-Webster Online Dictionary
amidase (noun)
an enzyme that hydrolyzes acid usually with the liberation of ammonia - amides
Amidase (Wikipedia)
amidase
Identifiers
EC number 3.5.1.4
CAS number 9012-56-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Amidase
PDB 1m22 EBI.jpg
x-ray structure of native peptide amidase from stenotrophomonas maltophilia at 1.4 a
Identifiers
Symbol Amidase
Pfam PF01425
InterPro IPR000120
PROSITE PDOC00494
SCOP 1ocm
SUPERFAMILY 1ocm
OPM superfamily 58
OPM protein 1mt5

In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide:

Amide hydrolysis Amidase.png

Thus, the two substrates of this enzyme are monocarboxylic acid amide and H2O, whereas its two products are monocarboxylate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation.

Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have a highly conserved C-terminal region rich in serine and glycine residues, but devoid of aspartic acid and histidine residues, therefore they differ from classical serine hydrolases. These enzymes possess a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes.

Examples of AS signature-containing enzymes include: