BRENDA - Enzyme Database show
show all sequences of 3.5.1.3

Rat liver omega-amidase. Kinetic evidence for an acyl-enzyme intermediate

Hersh, L.B.; Biochemistry 11, 2251-2256 (1972)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
hydroxylamine
uncompetitive activation
Rattus norvegicus
methanol
uncompetitive activation
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
2,2,2-Trifluoroethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
2-Chloroethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
dioxane
up to 5% dioxane: no effect on hydrolysis of ethyl alpha-keto-glutarate or glutaramate, at 10% dioxane: slight, 5-10% inhibition
Rattus norvegicus
ethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
methylamine
competitve inhibition, inhibits hydroxaminolysis of glutaramate and alpha-ketoglutaramate hydrolysis
Rattus norvegicus
additional information
no inhibition by ethylamine
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic studies, criteria and data
Rattus norvegicus
1
-
hydroxylamine
with substrate, acyl donor: p-methylphenyl glutarate
Rattus norvegicus
2
-
Glutaramate
hydrolysis
Rattus norvegicus
2
-
p-methylphenyl glutarate
hydrolysis
Rattus norvegicus
3
-
methyl glutarate
hydrolysis
Rattus norvegicus
3.7
-
hydroxylamine
with substrate, acyl donor: glutaramate
Rattus norvegicus
3.7
-
p-chlorophenyl glutarate
hydrolysis
Rattus norvegicus
4.1
-
hydroxylamine
with substrate, acyl donor: methyl glutarate
Rattus norvegicus
8
-
phenyl glutarate
hydrolysis
Rattus norvegicus
8
-
p-methoxyphenyl glutarate
hydrolysis
Rattus norvegicus
30
-
methylamine
with substrate, acyl donor: methyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
43
-
methylamine
with substrate, acyl donor: glutaramate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
55
-
methylamine
with substrate, acyl donor: p-methylphenyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
5000
-
methanol
with substrate, acyl donor: glutaramate
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxoglutaramate + H2O
Rattus norvegicus
alpha-ketoglutaramate
2-oxoglutarate + NH3
-
Rattus norvegicus
?
additional information
Rattus norvegicus
enzyme, in conjunction with glutamine transaminase comprises enzyme system previously designated glutaminase II, involved in metabolism of glutamine
?
-
-
-
Organic Solvent Stability
Organic Solvent
Commentary
Organism
2,2,2-trifluoroethanol
more than 2 M: unstable to
Rattus norvegicus
2-chloroethanol
more than 2 M: unstable to
Rattus norvegicus
Ethanol
more than 2 M: unstable to
Rattus norvegicus
Methanol
more than 2 M: stable to and uncompetitive activation
Rattus norvegicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Rattus norvegicus
Reaction
Reaction
Commentary
Organism
a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3
acyl-enzyme mechanism; catalytic sequence involves two steps and an acyl-enzyme intermediate; double displacement or ping-pong mechanism; kinetic evidence for an acyl-enzyme intermediate; two-step mechanism
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Rattus norvegicus
-
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
17.4
-
ethyl alpha-ketoglutarate hydrolysis
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxoglutaramate + H2O
alpha-ketoglutaramate
288888
Rattus norvegicus
2-oxoglutarate + NH3
-
288888
Rattus norvegicus
?
delta-ethyl 2-oxoglutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
gamma-ethyl 2-oxoglutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
glutaramate + H2O
-
288888
Rattus norvegicus
glutarate + NH3
-
-
-
?
glutaramate + hydroxylamine
-
288888
Rattus norvegicus
glutaryl hydroxamate + NH3
-
-
-
?
glutaramate + methanol
methanolysis
288888
Rattus norvegicus
glutarate methyl ester + hydroxylamine
-
-
-
?
glutaramate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
glutarate + hydroxylamine
acyl-transfer reaction
288888
Rattus norvegicus
glutaryl hydroxamate
-
-
-
?
methyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
methyl glutarate + hydoxylamine
-
288888
Rattus norvegicus
glutaramate + methanol
-
-
-
?
methyl glutarate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
additional information
substrate specificity
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydrolysis and acyl-transfer reactions with amide and monoalkyl esters of alpha-ketoglutarate, glutarate, and succinate
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes methanolysis, no alcoholysis using ethanol, 2-chloroethanol, and 2,2,2-trifluoroethanol
288888
Rattus norvegicus
?
-
-
-
-
additional information
rate of hydrolysis is decreased proportionally to the increase in hydroxaminolysis
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydroxaminolysis and transamidation reactions with esters and amides
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydrolysis and hydroxaminolysis
288888
Rattus norvegicus
?
-
-
-
-
additional information
enzyme, in conjunction with glutamine transaminase comprises enzyme system previously designated glutaminase II, involved in metabolism of glutamine
288888
Rattus norvegicus
?
-
-
-
-
p-chlorophenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methoxyphenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methylphenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methylphenyl glutarate + hydroxylamine
-
288888
Rattus norvegicus
glutaramate + 4-methylphenol
-
-
-
?
p-methylphenyl glutarate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
phenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
succinate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
p-methylphenyl glutarate hydrolysis and ethyl alpha-ketoglutarate hydrolysis, assay at
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
p-methylphenyl glutarate hydrolysis, assay at
Rattus norvegicus
7.4
-
ethyl alpha-keto-glutarate hydrolysis, assay at
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
hydroxylamine
uncompetitive activation
Rattus norvegicus
methanol
uncompetitive activation
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,2,2-Trifluoroethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
2-Chloroethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
dioxane
up to 5% dioxane: no effect on hydrolysis of ethyl alpha-keto-glutarate or glutaramate, at 10% dioxane: slight, 5-10% inhibition
Rattus norvegicus
ethanol
more than 2 M: irreversible inactivation
Rattus norvegicus
methylamine
competitve inhibition, inhibits hydroxaminolysis of glutaramate and alpha-ketoglutaramate hydrolysis
Rattus norvegicus
additional information
no inhibition by ethylamine
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic studies, criteria and data
Rattus norvegicus
1
-
hydroxylamine
with substrate, acyl donor: p-methylphenyl glutarate
Rattus norvegicus
2
-
Glutaramate
hydrolysis
Rattus norvegicus
2
-
p-methylphenyl glutarate
hydrolysis
Rattus norvegicus
3
-
methyl glutarate
hydrolysis
Rattus norvegicus
3.7
-
hydroxylamine
with substrate, acyl donor: glutaramate
Rattus norvegicus
3.7
-
p-chlorophenyl glutarate
hydrolysis
Rattus norvegicus
4.1
-
hydroxylamine
with substrate, acyl donor: methyl glutarate
Rattus norvegicus
8
-
phenyl glutarate
hydrolysis
Rattus norvegicus
8
-
p-methoxyphenyl glutarate
hydrolysis
Rattus norvegicus
30
-
methylamine
with substrate, acyl donor: methyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
43
-
methylamine
with substrate, acyl donor: glutaramate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
55
-
methylamine
with substrate, acyl donor: p-methylphenyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller
Rattus norvegicus
5000
-
methanol
with substrate, acyl donor: glutaramate
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxoglutaramate + H2O
Rattus norvegicus
alpha-ketoglutaramate
2-oxoglutarate + NH3
-
Rattus norvegicus
?
additional information
Rattus norvegicus
enzyme, in conjunction with glutamine transaminase comprises enzyme system previously designated glutaminase II, involved in metabolism of glutamine
?
-
-
-
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
2,2,2-trifluoroethanol
more than 2 M: unstable to
Rattus norvegicus
2-chloroethanol
more than 2 M: unstable to
Rattus norvegicus
Ethanol
more than 2 M: unstable to
Rattus norvegicus
Methanol
more than 2 M: stable to and uncompetitive activation
Rattus norvegicus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Rattus norvegicus
-
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
17.4
-
ethyl alpha-ketoglutarate hydrolysis
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxoglutaramate + H2O
alpha-ketoglutaramate
288888
Rattus norvegicus
2-oxoglutarate + NH3
-
288888
Rattus norvegicus
?
delta-ethyl 2-oxoglutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
gamma-ethyl 2-oxoglutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
glutaramate + H2O
-
288888
Rattus norvegicus
glutarate + NH3
-
-
-
?
glutaramate + hydroxylamine
-
288888
Rattus norvegicus
glutaryl hydroxamate + NH3
-
-
-
?
glutaramate + methanol
methanolysis
288888
Rattus norvegicus
glutarate methyl ester + hydroxylamine
-
-
-
?
glutaramate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
glutarate + hydroxylamine
acyl-transfer reaction
288888
Rattus norvegicus
glutaryl hydroxamate
-
-
-
?
methyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
methyl glutarate + hydoxylamine
-
288888
Rattus norvegicus
glutaramate + methanol
-
-
-
?
methyl glutarate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
additional information
substrate specificity
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydrolysis and acyl-transfer reactions with amide and monoalkyl esters of alpha-ketoglutarate, glutarate, and succinate
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes methanolysis, no alcoholysis using ethanol, 2-chloroethanol, and 2,2,2-trifluoroethanol
288888
Rattus norvegicus
?
-
-
-
-
additional information
rate of hydrolysis is decreased proportionally to the increase in hydroxaminolysis
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydroxaminolysis and transamidation reactions with esters and amides
288888
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes hydrolysis and hydroxaminolysis
288888
Rattus norvegicus
?
-
-
-
-
additional information
enzyme, in conjunction with glutamine transaminase comprises enzyme system previously designated glutaminase II, involved in metabolism of glutamine
288888
Rattus norvegicus
?
-
-
-
-
p-chlorophenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methoxyphenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methylphenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
p-methylphenyl glutarate + hydroxylamine
-
288888
Rattus norvegicus
glutaramate + 4-methylphenol
-
-
-
?
p-methylphenyl glutarate + methylamine
-
288888
Rattus norvegicus
?
-
-
-
?
phenyl glutarate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
succinate + H2O
-
288888
Rattus norvegicus
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
p-methylphenyl glutarate hydrolysis and ethyl alpha-ketoglutarate hydrolysis, assay at
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
p-methylphenyl glutarate hydrolysis, assay at
Rattus norvegicus
7.4
-
ethyl alpha-keto-glutarate hydrolysis, assay at
Rattus norvegicus
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
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-