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Information on EC 3.5.1.4 - amidase and Organism(s) Rhodococcus erythropolis and UniProt Accession P22984
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3.5.1.4 amidaseSpecify your search results
Word Map
- 3.5.1.4
-
deamination
- 1-aminocyclopropane-1-carboxylate
- peptidoglycan
- cytidine
- inosine
- esterase
- nitrile
-
siderophore
-
growth-promoting
- rhodococcus
-
hydratase
-
endocannabinoids
- cannabinoids
- iaa
- penicillin
-
hypermutation
- autolysins
-
endophytic
-
indole-3-acetic
-
rhizosphere
- rhizobacteria
- apobec3s
- deoxycytidine
-
editor
-
activation-induced
- porphobilinogen
- palmitoylethanolamide
-
a-to-i
- glucosamine-6-phosphate
- erythropolis
- porphyria
- 2-arachidonoylglycerol
- endolysins
- monoacylglycerol
- ehna
-
rna-specific
-
biofertilizer
-
dihydrolase
- uroporphyrinogens
-
polypeptide-like
- muropeptides
- deoxycytidylate
-
bacteriolytic
- 5-fluorocytosine
- dcmp
-
2\'-deoxycoformycin
-
diphosphohydrolase
- synthesis
- deoxycoformycin
-
pngase
-
ecto-5\'-nucleotidase
- drug development
- biotechnology
- environmental protection
- medicine
- industry
- pharmacology
The taxonomic range for the selected organisms is: Rhodococcus erythropolis
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid transferase
-
-
-
-
acylamidase
-
-
-
-
acylase
-
-
-
-
amidase
amide hydrolase
-
-
-
-
amide transferase
-
-
-
-
amidohydrolase
-
-
-
-
deaminase
-
-
-
-
ester transferase
-
-
-
-
N-acetylaminohydrolase
-
-
-
-
Wide spectrum amidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic acid amide
-
-
-
-
transfer of amide group
-
-
-
-
transfer of acyl group
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acylamide amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9012-56-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-chloromandelamide + H2O
(R)-2-chloromandelic acid + NH3
-
-
-
?
4-chloro-3-hydroxybutyramide + H2O
4-chloro-3-hydroxybutyrate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme
-
-
?
4-chloro-3-hydroxybutyramide + H2O
4-chloro-3-hydroxybutyric acid + NH3
-
-
-
?
acetamide + H2O
acetic acid + NH3
also acyl transfer activity in the presence of hydroxylamine
-
-
?
acrylamide + H2O
acrylic acid + NH3
also acyl transfer activity in the presence of hydroxylamine
-
-
?
benzamide + H2O
benzoic acid + NH3
also acyl transfer activity in the presence of hydroxylamine
-
-
?
butyramide + H2O
butyrate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme
-
-
?
isobutyramide + H2O
isobutyrate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme, preferred substrate
-
-
?
ketoprofen amide
2-(3-benzoylphenyl)propionic acid + NH3
-
-
-
?
propionamide + H2O
propionic acid + NH3
also acyl transfer activity in the presence of hydroxylamine
-
-
?
acetamide + H2O
acetate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme, low activity
-
-
?
acrylamide + H2O
acrylate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme
-
-
?
benzamide + H2O
benzoate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme
-
-
?
propionamide + H2O
propionate + NH3
-
substrate of the soluble enzyme and of the immobilized, cross-linked enzyme
-
-
?
additional information
?
-
the enzyme is absolutely enantioselective, biocatalytic hydrolysis of cyanohydrins of amidase with nitrile hydratase, overview
-
-
?
additional information
?
-
-
the enzyme is absolutely enantioselective, biocatalytic hydrolysis of cyanohydrins of amidase with nitrile hydratase, overview
-
-
?
additional information
?
-
enantioselectivity toward (R)-4-chloro-3-hydroxybutyramide: e.e value 52% (conversion yield 57%)
-
-
?
additional information
?
-
-
enantioselectivity toward (R)-4-chloro-3-hydroxybutyramide: e.e value 52% (conversion yield 57%)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ketoprofen amide
2-(3-benzoylphenyl)propionic acid + NH3
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.1
Acrylamide
-
pH and temperature not specified in the publication
1.03
Benzamide
-
pH and temperature not specified in the publication
34.2
Propionamide
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.2
acetamide
-
pH and temperature not specified in the publication
2.1
Acrylamide
-
pH and temperature not specified in the publication
157.7
Benzamide
-
pH and temperature not specified in the publication
155.2
Propionamide
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.14
acetamide
-
pH and temperature not specified in the publication
0.087
Acrylamide
-
pH and temperature not specified in the publication
153.5
Benzamide
-
pH and temperature not specified in the publication
4.54
Propionamide
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence identical to the sequenced enzyme fragment from strain NCIMB11540; NCIMB11540
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is involved in the nitrile hydratase pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
generation of an immobilized, cross-linked enzyme aggregate by mixing of the recombinant, crude, soluble enzyme with bovine serum albumin, and ammonium sulfate precipitation, followed by cross-linking of the resultant precipitant with glutaraldehyde. The enzyme aggregate shows hydrolytic activity toward a variety of amide substrates, and increased reaction stability
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
-
1 h, the enzyme maintains 100% of its original activity when incubated for 1 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion-exchange chromatography, phenyl-Superose column, desalted with a Hitrap desalting column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ami, expression in Bacillus subtilis and in Escherichia coli strain BL21 (DE3) using different promoters. Analysis of expression effect of different promoters in Bacillus subtilis using five distinct promoters, sacB, amyE, p43, degQ, aprE, and their native signal peptide genes, to separately construct five different vectors harboring ami gene, overview. The amyE promoter along with its native signal peptide gene is most effective
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
the enzyme is useful in biocatalytic nitrile hydrolysis in a system together with nitrile hydratase, EC 4.2.1.84
industry
-
the immobilized, cross-linked enzyme aggregate proves useful as a substitute for soluble amidase as a biocatalyst in the pharmaceutical and chemical industries
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirrlinger, B.; Stolz, A.; Knackmuss, H.J.
Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides
J. Bacteriol.
178
3501-3507
1996
Rhodococcus erythropolis, Rhodococcus erythropolis MP50
Reisinger, C.; Osprian, I.; Glieder, A.; Schoemaker, H.E.; Griengl, H.; Schwab, H.
Enzymatic hydrolysis of cyanohydrins with recombinant nitrile hydratase and amidase from Rhodococcus erythropolis
Biotechnol. Lett.
26
1675-1680
2004
Rhodococcus erythropolis (P22984), Rhodococcus erythropolis, Rhodococcus erythropolis NCIMB11540 (P22984)
Vaidya, B.K.; Mutalik, S.R.; Joshi, R.M.; Nene, S.N.; Kulkarni, B.D.
Enhanced production of amidase from Rhodococcus erythropolis MTCC 1526 by medium optimisation using a statistical experimental design
J. Ind. Microbiol. Biotechnol.
36
671-678
2009
Rhodococcus erythropolis
Park, H.J.; Uhm, K.N.; Kim, H.K.
R-stereoselective amidase from Rhodococcus erythropolis No. 7 acting on 4-chloro-3-hydroxybutyramide
J. Microbiol. Biotechnol.
18
552-559
2008
Rhodococcus erythropolis (B4XEY3), Rhodococcus erythropolis, Rhodococcus erythropolis No. 7 (B4XEY3)
Han, W.W.; Wang, Y.; Zhou, Y.H.; Yao, Y.; Li, Z.S.; Feng, Y.
Understanding structural/functional properties of amidase from Rhodococcus erythropolis by computational approaches
J. Mol. Model.
15
481-487
2009
Rhodococcus erythropolis (P22984), Rhodococcus erythropolis
Park, H.J.; Uhm, K.N.; Kim, H.K.
Biotransformation of amides to acids using a co-cross-linked enzyme aggregate of Rhodococcus erythropolis amidase
J. Microbiol. Biotechnol.
20
325-331
2010
Rhodococcus erythropolis
Yue, Y.; Lian, J.; Tian, P.; Tan, T.
Cloning of amidase gene from Rhodococcus erythropolis and expression by distinct promoters in Bacillus subtilis
J. Mol. Catal. B
56
89-95
2009
Rhodococcus erythropolis
-
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