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3.5.1.4: amidase

This is an abbreviated version!
For detailed information about amidase, go to the full flat file.

Word Map on EC 3.5.1.4

Reaction

a monocarboxylic acid amide
+
H2O
=
a monocarboxylate
+
NH3

Synonyms

4-guanidinobutyramide hydrolase, A-amidase, acetamidase, acid transferase, acylamidase, acylase, AMI1, amidase, amidase 1, amide hydrolase, amide transferase, amidohydrolase, AmiE, Ana, anandamide hydrolase, AtFAAH, Azl13, C-amidase, deaminase, ester transferase, FAAH, FAAH-1, FAAH-2, fatty acid amide hydrolase, fatty acid amide hydrolase 1, fatty acylamidase, half-amidase, indole-3-acetamide amidohydrolase, K1, mHG, Mhpg, More, murein peptide amidase A, mycothiol-S-conjugate amidase, N-acetylaminohydrolase, N-acylethanolamine acid amidase, N-acylethanolamine-hydrolyzing acid amidase, N-acylethanolaminehydrolyzing acid amidase, NAAA, NAE-hydrolyzing acid amidase, PamH, PYCH_10400, R-stereospecific amidase, RhAmidase, signature amidase, SsAH, SSAM, SSO2122, tissue kallikrein, Wide spectrum amidase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.4 amidase

Purification

Purification on EC 3.5.1.4 - amidase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a. transformant : sonication, lysis, dialysis against urea, b. wild-type amidase: dialysis, Mono-Q HR 5/5 column, ammonium sulfate precipitation, dialysis
-
acetone precipitation, ammonium sulfate fractionation, DEAE-Sepharose chromatography, Mono Q column and gel filtration, purified approximately 138fold with a yield of 20%
-
acetone precipitation, DEAE-Sepharose, ammonium sulfate precipitation, yield 10%
-
affinity chromatography on an acetamide epoxy-activated Sepharose column
affinity chromatography on epoxy-activated Sepharose 6B-acetamide and gel filtration
-
ammonium sulfate precipitation and dialysis and gel filtration on DEAE-Sephadex A-50
-
ammonium sulfate precipitation, 30 to 55%, and hydrophobic, anion-exchange, gel filtration, and ceramic hydroxyapatite chromatography steps, DTT required to maintain enzymatic activity, overall level of purification 114-fold, recovery rate 21%
-
cell extract purified by DEAE-Sephacel column, concentrated by ultrafiltration, phenyl-Sepharose column, Sephacryl S-200 column, Mono Q HR 5/5 and Mono Q PC 1.6/5 column
Blastobacter sp.
-
dialysis, column chromatography and ammonium sulfate fractionation
-
enriched 48fold by fractional precipitation with ammonium sulfate, Sephadex gel filtration and anion exchange chromatography
-
extraction of a His-tagged enzyme from insoluble cellular fractions using sodium phosphate buffer at pH 7.8 and further purification by affinity column chromatography
-
FAA II : supernant concentrated by Amicon filter, purified by DEAE-cellulose, ammonium sulfate precipitation, gel filtration and SDS-PAGE
-
from male urine to homogeneity
-
heat precipitation and S-300 gel filtration
-
ion-exchange chromatography, phenyl-Superose column, desalted with a Hitrap desalting column
-
lysis of crude extract, addition of streptomycin, ammonium sulfate fractionation, desalting by Sephadex-gel filtration, DEAE-Sepharose chromatography, hydroxyapatite column, yield 72%
-
native enzyme 11.15fold to homogeneity by two steps of anion exchange chromatography, followed by gel filtration
-
native enzyme 11.2fold by anion exchange chromatography, and gel filtration
-
native enzyme 2.9fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
-
native enzyme 48fold to homogeneity by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, and gel filtration
-
native enzyme 52.04fold to homogeneity by heat treatment, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme 6.2fold to apparent homogeneity by anion exchange chromatography and gel filtration
-
partially by membrane fraction preparation
-
passage with French pressure cell, cell-free extract purified and concentrated by using anion-exchange and gel filtration, judged by SDS-PAGE and scanning densiometry
-
preparation of cell-free extracts by sonification, DEAE-Sephacel column chromatography, ammonium sulfate fraction, Mono-Q column chromatography, Superose 12 column chromatography, yield 30.4%
-
prepared of a crude extract by ultrasonic treatment, purification and concentration with ion-exchange chromatography, hydrophobic chromatography, hydroxyapatite chromatography
-
purified in a single-step procedure using a choline-Sepharose 6B column
-
recombinant enzyme 2.35fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography
-
recombinant enzyme partially from Escherichia coli strain XL-1 Blue by heat treatment of the cell-free extract
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to 99% homogeneity
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged wild-type enzyme 5.82fold from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, dialysis, anion exchange chromatography, gel filtration, and ultrafiltration
recombinant insoluble aggregated His6-tagged protein from Escherichia coli by denaturation, refolding during nickel affinity chromatography, gel filtration, and heat treatment, 2.9fold to homogeneity
-
recombinant wild-type and mutant enzymes by acetamide affinity chromatography and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli by acetamide affinity chromatography and gel filtration
-
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21 by anion exchange chromatography, ammonium sulfate fractionation, and a second different step of anion exchange chromatography
several chromatographic steps, including Q-Sepharose and Sephacryl S-100
strain PPW3, C-amidase, ammonium sulfate fractionation, gel filtration, DEAE-Sephadex, preparative PAGE, purification factor 40
-
streptomycin sulfate treatment, a heat treatment, ammonium sulfate fractionation and column chromatography on DEAE-Sephadex , yield 30%, purification was 19fold
-
using affinity column chromatography
-
wild-type enzyme by acetamide affinity chromatography and gel filtration
-