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Information on EC 3.5.1.4 - amidase and Organism(s) Alcaligenes sp. and UniProt Accession Q70I53

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.4 amidase
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Select one or more organisms in this record: ?
This record set is specific for:
Alcaligenes sp.
UNIPROT: Q70I53 not found.
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Word Map
The taxonomic range for the selected organisms is: Alcaligenes sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
amidase, deaminase, acylase, acetamidase, amide hydrolase, acid transferase, n-acylethanolamine acid amidase, n-acylethanolamine-hydrolyzing acid amidase, atfaah, acylamidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid transferase
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acylamidase
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acylase
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amide hydrolase
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amide transferase
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amidohydrolase
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deaminase
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ester transferase
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N-acetylaminohydrolase
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Wide spectrum amidase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic acid amide
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transfer of amide group
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transfer of acyl group
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hydrolysis of carboxylic acid amide
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transfer of amide group
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transfer of acyl group
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SYSTEMATIC NAME
IUBMB Comments
acylamide amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9012-56-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate-prelabeled chicken histones + H2O
deacetylated chicken histones + acetate
show the reaction diagram
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-
-
?
acetylcadaverine + H2O
acetate + cadaverine
show the reaction diagram
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-
-
?
acetylputrescine + H2O
acetate + putrescine
show the reaction diagram
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-
-
?
acetylspermidine + H2O
acetate + spermidine
show the reaction diagram
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-
-
?
Boc-Lys(epsilon-acetyl)-(4-methyl-coumaryl-7-amide) + H2O
Boc-Lys-(4-methyl-coumaryl-7-amide) + acetate
show the reaction diagram
-
-
-
?
cis-(1S,4R)-N-(4-(hydroxymethyl)cyclopent-2-enyl)acetamide + H2O
cis-(1S,4R)-(4-(hydroxymethyl)cyclopent-2-enyl)amine + acetate
show the reaction diagram
used as enzymatic assay
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-
?
additional information
?
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the amidase of the organism exhibits dual activity i.e. hydrolase as well as acyl transfer. The acyl transfer activity of amidase forms an hydroxamate and ammonia from an amide and hydroxylamine and shows broader substrate affinity ranging from a variety of aliphatic amides (formamide, acetamide, propanamide etc.) to aromatic amides (benzamide, mandelamide, nicotinamide etc.) along with hydroxylamine for the biotransformation of these amides into corresponding hydroxamic acid, substrate specificity, overview
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activation above 100 mM
Co2+
increases 1.3fold the activity at 1 mM, inhibition at higher concentration
Mg2+
activation above 100 mM
Mn2+
activation above 100 mM
Ni2+
increases 1.1fold the activity at 1 mM, inhibition at higher concentration
Zn2+
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
suberoylanilide hydroxamic acid
strong inhibition
tricostatin A
strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
acetate-prelabeled chicken histones
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0.127
Boc-Lys(epsilon-acetyl)-(4-methyl-coumaryl-7-amide)
pH 7.5, 37°C
4
cis-(1S,4R)-N-(4-(hydroxymethyl)cyclopent-2-enyl)acetamide
pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
acetylspermidine, pH 7.5
0.008
acetylcadaverine, pH 7.5
0.011
acetylputrescine, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain FB188, or Bordetella sp.
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39420
from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1* 35000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
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quite stable at 50°C with t1/2 of 8 h, at 60°C t1/2 is 90 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
several chromatographic steps, including Q-Sepharose and Sephacryl S-100
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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the acyl transfer activity of the enzyme can be used for the synthesis of variety of hydroxamic acids. Optimization of physiochemical parameters result into 30fold increase in the acyl transfer activity of amidase. The acyl transfer activity of amidase of Alcaligenes sp. MTCC 10674 under high temperature condition makes of potential application in developing a bioprocess for the production of variety of aliphatic and aromatic hydroxamic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hildmann, C.; Ninkovic, M.; Dietrich, R.; Wegener, D.; Riester, D.; Zimmermann, T.; Birch, O.M.; Bernegger, C.; Loidl, P.; Schwienhorst, A.
A new amidohydrolase from Bordetella or Alcaligenes strain FB188 with similarities to histone deacetylases
J. Bacteriol.
186
2328-2339
2004
Alcaligenes sp. (Q70I53), Alcaligenes sp. DSM 11172 (Q70I53)
Manually annotated by BRENDA team
Kant, B.; Kant, B.; Kumar, M.; Chand, B.
Production and characterization of acyl transfer activity of amidase from Alcaligenes sp. MTCC 10674 for synthesis of hydroxamic acids
J. Microb. Biochem. Technol.
5
1-5
2013
Alcaligenes sp., Alcaligenes sp. MTCC 10674
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Manually annotated by BRENDA team