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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/09/11 05:06:56」(JST)

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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:

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.^[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 source | edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2PLQ and 2UXY.

References[edit source | edit]

^ ^a ^b ValiÃ±a 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.
^ 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.
^ 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.
^ 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.

English Journal

Effect of growth media on cell envelope composition and nitrile hydratase stability in Rhodococcus rhodochrous strain DAP 96253.

Tucker TA, Crow SA Jr, Pierce GE.SourceGeorgia State University, 24 Peachtree Center Ave, Atlanta, GA, 30303, USA, biotmt@langate.gsu.edu.
Journal of industrial microbiology & biotechnology.J Ind Microbiol Biotechnol.2012 Nov;39(11):1577-85. doi: 10.1007/s10295-012-1168-z. Epub 2012 Jul 29.
Rhodococcus is an important industrial microorganism that possesses diverse metabolic capabilities; it also has a cell envelope, composed of an outer layer of mycolic acids and glycolipids. Selected Rhodococcus species when induced are capable of transforming nitriles to the corresponding amide by t
PMID 22842987

Functional expression of trypsin from Streptomyces griseus by Pichia pastoris.

Ling Z, Ma T, Li J, Du G, Kang Z, Chen J.SourceThe Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi, 214122, China.
Journal of industrial microbiology & biotechnology.J Ind Microbiol Biotechnol.2012 Nov;39(11):1651-62. doi: 10.1007/s10295-012-1172-3. Epub 2012 Jul 28.
In the present study, the genes encoding trypsinogen and active trypsin from Streptomyces griseus were both cloned and expressed in the methylotrophic yeast Pichia pastoris with the α-factor secretion signal under the control of the alcohol oxidase promoter. The mature trypsin was successfully accu
PMID 22842958

Japanese Journal

Biochemical Features of a Catalytic Antibody Light Chain, 22F6, Prepared from Human Lymphocytes

Hifumi Emi,Fujimoto Naoko,Arakawa Mitsue,Saito Eri,Matsumoto Shingo,Kobayashi Nobuyuki,Uda Taizo
Journal of Biological Chemistry 288(27), 19558-19568, 2013-07-05
… The light chain cleaved a peptide bond of synthetic peptidyl-4-methylcoumaryl- 7-amide (MCA) substrates, such as QAR-MCA and EAR-MCA, indicating amidase activity. … From the analysis of amino acid sequences and molecular modeling, the 22F6 light chain possesses two kinds of active sites as amidase and nuclease in close distances. …
NAID 120005317134

Application of protein N-terminal amidase in enzymatic synthesis of dipeptides containing acidic amino acids specifically at the N-terminus

ARAI Toshinobu,NOGUCHI Atsushi,TAKANO Eriko,KINO Kuniki
Journal of bioscience and bioengineering 115(4), 382-387, 2013-04-25
NAID 10031186935

Application of protein N-terminal amidase in enzymatic synthesis of dipeptides containing acidic amino acids specifically at the N-terminus(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Arai Toshinobu,Noguchi Atsushi,Takano Eriko [他],Kino Kuniki
Journal of bioscience and bioengineering 115(4), 382-387, 2013-04
… and Xaa, arbitrary amino acids) synthesized by Lals were continuously deamidated by a novel amidase, yielding Asp-Xaa and Glu-Xaa (Asp, L-aspartic acid; … We focused on the protein N-terminal amidase from Saccharomyces cerevisiae (NTA1), and assayed its activity toward dipeptides. …
NAID 110009603684

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★リンクテーブル★

リンク元	「acylase」「アミダーゼ」「amidohydrolase」
拡張検索	「peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase」「acylamidase」「glucosylceramidase deficiency」「nicotinamidase」

「acylase」

Amidase
	; 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	72
OPM protein	1mt5
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

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
Search
PMC	articles
PubMed	articles
NCBI	proteins