amidase

Identifiers
EC no.| 3.5.1.4
CAS no.| 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  / QuickGO
| Search

PMC| articles
PubMed| articles
NCBI| proteins

Protein family

Amidase

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 Å

Identifiers
Symbol| Amidase
Pfam| PF01425
InterPro| IPR000120
PROSITE| PDOC00494
SCOP2| 1ocm / SCOPe / SUPFAM
OPM superfamily| 55
OPM protein| 1mt5
Membranome| 325
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

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. In this way, 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:

* Peptide amidase (Pam),[1] which catalyses the hydrolysis of the C-terminal amide bond of peptides.
* Fatty acid amide hydrolases,[2] which hydrolyse fatty acid amid substrates (e.g. cannabinoid anandamide and sleep-inducing oleamide), thereby controlling the level and duration of signalling induced by this diverse class of lipid transmitters.
* Malonamidase E2,[3] which catalyses the hydrolysis of malonamate into malonate and ammonia, and which is involved in the transport of fixed nitrogen from bacteroids to plant cells in symbiotic nitrogen metabolism.
* Subunit A of Glu-tRNA(Gln) amidotransferase,[4] a heterotrimeric enzyme that catalyses the formation of Gln-tRNA(Gln) by the transamidation of misacylated Glu-tRNA(Gln) via amidolysis of glutamine.

## Structural studies

[edit]

This section needs to be updated. Please help update this article to reflect recent events or newly available information. (May 2017)

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As of late 2018, 162 structures have been solved for this family, which can be accessed at the Pfam Archived 2021-09-18 at the Wayback Machine.

## References

[edit]

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\. doi:10.1016/S1016-8478(23)15118-1. PMID 12521300.

## Further reading

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* Bray HG, James SP, Raffan IM, Ryman BE, Thorpe WV (1949). "The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver". Biochem. J. 44 (5): 618–625\. doi:10.1042/bj0440618. PMC 1274617.
* Bray HG, James SP, Thorpe WV, Wasdell MR (1950). "The fate of certain organic acids and amides in the rabbit. 11 Further observations on the hydrolysis of amides by tissue extracts". Biochem. J. 47 (3): 294–299\. doi:10.1042/bj0470294. PMC 1275209. PMID 14800883.

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Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides /
Amidohydrolases|

* Asparaginase
* Glutaminase
* Urease
* Biotinidase
* Aminoacylase
* ACY1
* Aspartoacylase(ACY2)
* ACY3
* Ceramidase
* Aspartylglucosaminidase
* Fatty acid amide hydrolase
* Histone deacetylase
* Sirtuin

3.5.2: Cyclic amides/
Amidohydrolases|

* Barbiturase
* Beta-lactamase
* Dihydroorotase

3.5.3: Linear amidines/
Ureohydrolases|

* Arginase
* Agmatinase
* Protein-arginine deiminase

3.5.4: Cyclic amidines/
Aminohydrolases|

* Guanine deaminase
* Adenosine deaminase
* AMP deaminase
* Inosine monophosphate synthase
* DCMP deaminase
* GTP cyclohydrolase I
* Cytidine deaminase
* AICDA
* Activation-induced cytidine deaminase

3.5.5: Nitriles/
Aminohydrolases|

* Nitrilase

3.5.99: Other|

* Riboflavinase
* Thiaminase II

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

Portal:

* Biology

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

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