BRENDA - Enzyme Database show
show all sequences of 3.5.1.3

Dicarboxylate omega-amidase of Bacillus subtilis-168: evidence for a membrane-associated form

Ramaley, R.F.; Fernald, N.; DeVries, T.; Arch. Biochem. Biophys. 153, 88-94 (1972)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
sodium deoxycholate
membrane-associated form
Bacillus subtilis
sodium lauryl sulfate
membrane-associated form
Bacillus subtilis
Triton X-100
membrane-associated form
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
NH4+
biosynthesis of omega-amidase is repressed by free ammonium ions; biosynthesis of omega-amidase strongly repressed by ammonia, 0.001 M: 98% repression, 0.005 M: complete repression, ammonia has no effect on catalytic activity: succinyl hydroxamate formation
Bacillus subtilis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Bacillus subtilis
5737
-
membrane
membrane-associated, one third to one fourth of total omega-amidase; not covalently bound to membrane
Bacillus subtilis
16020
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
168, wild-type
-
Bacillus subtilis 168
-
168, wild-type
-
Purification (Commentary)
Commentary
Organism
partial, membrane-associated, with detergents
Bacillus subtilis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.59
-
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinamate + hydroxylamine
-
288887
Bacillus subtilis
succinyl hydroxamate + NH3
-
-
-
r
succinamate + hydroxylamine
-
288887
Bacillus subtilis 168
succinyl hydroxamate + NH3
-
-
-
r
succinate + hydroxylamine
-
288887
Bacillus subtilis
succinyl hydroxamate + H2O
-
-
-
r
succinate + hydroxylamine
-
288887
Bacillus subtilis 168
succinyl hydroxamate + H2O
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
sodium deoxycholate
membrane-associated form
Bacillus subtilis
sodium lauryl sulfate
membrane-associated form
Bacillus subtilis
Triton X-100
membrane-associated form
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
NH4+
biosynthesis of omega-amidase is repressed by free ammonium ions; biosynthesis of omega-amidase strongly repressed by ammonia, 0.001 M: 98% repression, 0.005 M: complete repression, ammonia has no effect on catalytic activity: succinyl hydroxamate formation
Bacillus subtilis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Bacillus subtilis
5737
-
membrane
membrane-associated, one third to one fourth of total omega-amidase; not covalently bound to membrane
Bacillus subtilis
16020
-
Purification (Commentary) (protein specific)
Commentary
Organism
partial, membrane-associated, with detergents
Bacillus subtilis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.59
-
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinamate + hydroxylamine
-
288887
Bacillus subtilis
succinyl hydroxamate + NH3
-
-
-
r
succinamate + hydroxylamine
-
288887
Bacillus subtilis 168
succinyl hydroxamate + NH3
-
-
-
r
succinate + hydroxylamine
-
288887
Bacillus subtilis
succinyl hydroxamate + H2O
-
-
-
r
succinate + hydroxylamine
-
288887
Bacillus subtilis 168
succinyl hydroxamate + H2O
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Other publictions for EC 3.5.1.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734871
Zhang
Identification and characteriz ...
Arabidopsis thaliana, Arabidopsis thaliana Col
Phytochemistry
99
36-43
2014
-
-
1
-
-
-
-
3
2
-
2
2
-
5
-
-
1
-
-
1
-
-
10
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
2
-
2
2
-
-
-
1
-
1
-
-
10
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
721018
Cobzaru
Homologous gene clusters of ni ...
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499, Paenarthrobacter nicotinovorans, Rhodococcus opacus
Res. Microbiol.
162
285-291
2011
-
-
2
-
-
-
-
-
-
-
-
4
-
8
-
-
-
-
-
-
-
-
5
-
3
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3
-
-
-
-
-
-
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2
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-
4
-
-
-
-
-
-
-
-
5
-
3
-
-
-
3
-
-
-
-
6
6
-
-
-
710840
Krasnikov
Assay and purification of omeg ...
Rattus norvegicus
Anal. Biochem.
391
144-150
2009
-
1
-
-
-
-
-
-
4
-
1
-
-
4
-
-
1
-
-
4
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
1
-
4
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
711316
Jaisson
Molecular identification of om ...
Mus musculus
Biochimie
91
1066-1071
2009
-
-
1
-
-
-
-
8
-
-
-
-
-
5
-
-
1
-
-
1
-
-
6
-
1
-
-
8
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
1
-
1
-
-
6
-
1
-
-
8
2
-
-
-
-
-
-
-
8
8
711317
Krasnikov
Identification of the putative ...
Homo sapiens, Rattus norvegicus
Biochimie
91
1072-1080
2009
-
-
1
-
-
-
-
3
-
-
8
4
-
4
-
-
2
-
-
3
-
-
4
2
2
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
8
4
-
-
-
2
-
3
-
-
4
2
2
-
-
-
2
-
-
-
-
1
1
-
-
-
288890
Makar
Glutamine transaminase K and o ...
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus
J. Neurochem.
62
1983-1988
1994
-
-
-
-
-
-
-
-
-
-
-
8
-
8
-
-
-
-
-
20
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
20
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288891
Cooper
High activities of glutamine t ...
Rattus norvegicus
J. Neurochem.
61
1731-1741
1993
-
-
-
-
-
-
-
-
3
-
-
5
-
4
-
-
-
-
-
7
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
5
-
-
-
-
-
7
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288884
Cooper
alpha-Keto acid omega-amidase ...
Embryophyta, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae
Methods Enzymol.
113
350-358
1985
-
3
-
-
-
2
8
3
5
1
2
8
-
6
1
-
1
1
1
13
2
2
24
1
-
-
3
-
2
-
-
-
-
-
-
-
3
-
-
-
-
2
-
8
-
3
5
1
2
8
-
1
-
1
1
13
2
2
24
1
-
-
3
-
2
-
-
-
-
-
-
-
-
-
288885
Calderon
omega-Amidase pathway in the d ...
Neurospora crassa
J. Bacteriol.
161
807-809
1985
-
-
-
-
-
-
3
-
-
-
-
2
-
2
-
-
-
-
-
-
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
288893
Cooper
The glutamine transaminase-ome ...
Canis lupus familiaris, Embryophyta, Enterococcus faecalis, Escherichia coli, Homo sapiens, Lactuca sativa, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Spinacia oleracea
CRC Crit. Rev. Biochem.
4
281-303
1977
-
-
-
-
-
-
-
-
3
-
1
11
-
10
-
-
1
1
-
20
-
-
36
1
-
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
11
-
-
-
1
-
20
-
-
36
1
-
-
1
-
3
-
1
-
-
-
-
-
-
-
288894
Cooper
The glutamine transaminase-ome ...
Homo sapiens, Rattus norvegicus
J. Neurochem.
28
771-778
1977
-
-
-
-
-
-
-
-
6
-
-
6
-
2
-
-
-
-
-
9
2
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
6
-
-
-
-
-
9
2
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
288886
Fernald
Purification and properties of ...
Bacillus subtilis 168, Bacillus subtilis, Thermus aquaticus, Thermus aquaticus YT-1
Arch. Biochem. Biophys.
153
95-104
1972
2
-
-
-
-
2
6
6
-
2
2
4
-
109
-
-
2
-
-
-
2
2
48
-
4
2
-
-
6
-
-
2
-
-
-
2
-
-
2
-
-
2
-
6
-
6
-
2
2
4
-
-
-
2
-
-
2
2
48
-
4
2
-
-
6
-
-
-
-
-
-
-
-
-
288887
Ramaley
Dicarboxylate omega-amidase of ...
Bacillus subtilis 168, Bacillus subtilis
Arch. Biochem. Biophys.
153
88-94
1972
3
-
-
-
-
-
1
-
2
-
-
-
-
89
-
-
1
-
-
-
1
-
4
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
1
-
-
1
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
288888
Hersh
Rat liver omega-amidase. Kinet ...
Rattus norvegicus
Biochemistry
11
2251-2256
1972
2
-
-
-
-
-
6
14
-
-
-
2
4
1
-
-
1
1
-
2
1
-
26
-
1
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
6
-
14
-
-
-
2
4
-
-
1
-
2
1
-
26
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
288892
Hersh
Rat liver omega-amidase. Purof ...
Rattus norvegicus
Biochemistry
10
2884-2891
1971
-
-
-
-
-
-
12
23
1
1
1
4
-
2
-
-
1
1
-
2
2
1
49
1
1
-
2
-
2
-
4
-
-
-
-
-
-
-
-
-
-
-
-
12
-
23
1
1
1
4
-
-
-
1
-
2
2
1
49
1
1
-
2
-
2
-
4
-
-
-
-
-
-
-
288889
Meister
Hydrolysis and transfer reacti ...
Rattus norvegicus
J. Biol. Chem.
215
441-460
1955
1
-
-
-
-
-
-
-
1
1
-
1
-
1
-
-
1
1
-
2
-
-
24
-
-
-
-
-
6
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
-
1
1
-
1
-
-
-
1
-
2
-
-
24
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-