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:

amidase
Identifiers
EC no.3.5.1.4
CAS no.9012-56-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Amidase
PDB 1m22 EBI.jpg
x-ray structure of native peptide amidase from stenotrophomonas maltophilia at 1.4 a
Identifiers
SymbolAmidase
PfamPF01425
InterProIPR000120
PROSITEPDOC00494
SCOP21ocm / SCOPe / SUPFAM
OPM superfamily55
OPM protein1mt5
Membranome325
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Amide hydrolysis Amidase.png

Thus, the two substrates of this enzyme are an 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.[1]

Examples of AS signature-containing enzymes include:

Structural studiesEdit

As of late 2018, 162 structures have been solved for this family, which can be accessed at the Pfam.

ReferencesEdit

  1. ^ a b Valiña AL, Mazumder-Shivakumar D, Bruice TC (December 2004). "Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate". Biochemistry. 43 (50): 15657–72. doi:10.1021/bi049025r. PMID 15595822.
  2. ^ Wei BQ, Mikkelsen TS, McKinney MK, Lander ES, Cravatt BF (December 2006). "A second fatty acid amide hydrolase with variable distribution among placental mammals". J. Biol. Chem. 281 (48): 36569–78. doi:10.1074/jbc.M606646200. PMID 17015445.
  3. ^ Shin S, Lee TH, Ha NC, Koo HM, Kim SY, Lee HS, Kim YS, Oh BH (June 2002). "Structure of malonamidase E2 reveals a novelSer-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature". EMBO J. 21 (11): 2509–16. doi:10.1093/emboj/21.11.2509. PMC 126024. PMID 12032064.
  4. ^ Kwak JH, Shin K, Woo JS, Kim MK, Kim SI, Eom SH, Hong KW (December 2002). "Expression, purification, and crystallization of glutamyl-tRNA(Gln) specific amidotransferase from Bacillus stearothermophilus". Mol. Cells. 14 (3): 374–81. PMID 12521300.

Further readingEdit

This article incorporates text from the public domain Pfam and InterPro: IPR000120