BRENDA - Enzyme Database
show all sequences of 3.5.1.55

Purification and characterisation of long chain acyl aminoacylase from Penicillium sp. B-001

Murase, H.; Kunieda, T.; Terao, J.; Nagao, A.; Biosci. Biotechnol. Biochem. 57, 854-855 (1993)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
DTT
-
Penicillium sp.
Hg2+
95% inhibition
Penicillium sp.
PCMB
-
Penicillium sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
N-oleoyl-L-glutamate
-
Penicillium sp.
0.21
-
N-oleolyl-L-glutamate
-
Penicillium sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Penicillium sp.
Cd2+
activates
Penicillium sp.
Cu2+
activates
Penicillium sp.
Mg2+
activates
Penicillium sp.
Ni2+
activates
Penicillium sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
192000
-
gel filtration
Penicillium sp.
Organism
Organism
UniProt
Commentary
Textmining
Penicillium sp.
-
-
-
Penicillium sp. B-001
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Penicillium sp.
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Penicillium sp.
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
624.5
-
-
Penicillium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
not: acetyl-L-glutamate
209199
Penicillium sp.
?
-
-
-
?
additional information
not: acetyl-L-glutamate
209199
Penicillium sp. B-001
?
-
-
-
?
N-arachidonoyl-L-glutamate + H2O
32% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
arachidonate + L-glutamate
-
209199
Penicillium sp.
?
N-benzoyl-L-glutamate + H2O
74% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
benzoate + L-glutamate
-
209199
Penicillium sp.
?
N-decanoyl-L-glutamate + H2O
best substrate
209199
Penicillium sp.
decanoate + L-glutamate
-
209199
Penicillium sp.
?
N-decanoyl-L-glutamate + H2O
best substrate
209199
Penicillium sp. B-001
decanoate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-lauroyl-L-glutamate + H2O
88% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
lauroate + L-glutamate
-
209199
Penicillium sp.
?
N-lauroyl-L-glutamate + H2O
88% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp. B-001
lauroate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-myristoyl-L-glutamate + H2O
-
209199
Penicillium sp.
myristoate + L-glutamate
-
209199
Penicillium sp.
?
N-myristoyl-L-glutamate + H2O
-
209199
Penicillium sp. B-001
myristoate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-octanoyl-L-glutamate + H2O
80% of the activity with decanoyl-L-glutamate
209199
Penicillium sp.
octanoate + L-glutamate
-
209199
Penicillium sp.
?
N-oleolyl-L-glutamate + H2O
-
209199
Penicillium sp.
oleate + L-glutamate
-
-
-
?
N-oleoyl-L-glutamate + H2O
67% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
oleate + L-glutamate
-
209199
Penicillium sp.
?
N-palmitoyl-L-glutamate + H2O
49% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
palmitate + L-glutamate
-
-
-
?
N-palmitoyl-L-glutamate + H2O
49% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp. B-001
palmitate + L-glutamate
-
-
-
?
N-stearoyl-L-glutamate + H2O
67% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
stearate + L-glutamate
-
209199
Penicillium sp.
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
pH 8.0, 15 min, stable
Penicillium sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Penicillium sp.
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
8
30°C, 5 h, stable
Penicillium sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
DTT
-
Penicillium sp.
Hg2+
95% inhibition
Penicillium sp.
PCMB
-
Penicillium sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
N-oleoyl-L-glutamate
-
Penicillium sp.
0.21
-
N-oleolyl-L-glutamate
-
Penicillium sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Penicillium sp.
Cd2+
activates
Penicillium sp.
Cu2+
activates
Penicillium sp.
Mg2+
activates
Penicillium sp.
Ni2+
activates
Penicillium sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
192000
-
gel filtration
Penicillium sp.
Purification (Commentary) (protein specific)
Commentary
Organism
-
Penicillium sp.
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Penicillium sp.
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
624.5
-
-
Penicillium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
not: acetyl-L-glutamate
209199
Penicillium sp.
?
-
-
-
?
additional information
not: acetyl-L-glutamate
209199
Penicillium sp. B-001
?
-
-
-
?
N-arachidonoyl-L-glutamate + H2O
32% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
arachidonate + L-glutamate
-
209199
Penicillium sp.
?
N-benzoyl-L-glutamate + H2O
74% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
benzoate + L-glutamate
-
209199
Penicillium sp.
?
N-decanoyl-L-glutamate + H2O
best substrate
209199
Penicillium sp.
decanoate + L-glutamate
-
209199
Penicillium sp.
?
N-decanoyl-L-glutamate + H2O
best substrate
209199
Penicillium sp. B-001
decanoate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-lauroyl-L-glutamate + H2O
88% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
lauroate + L-glutamate
-
209199
Penicillium sp.
?
N-lauroyl-L-glutamate + H2O
88% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp. B-001
lauroate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-myristoyl-L-glutamate + H2O
-
209199
Penicillium sp.
myristoate + L-glutamate
-
209199
Penicillium sp.
?
N-myristoyl-L-glutamate + H2O
-
209199
Penicillium sp. B-001
myristoate + L-glutamate
-
209199
Penicillium sp. B-001
?
N-octanoyl-L-glutamate + H2O
80% of the activity with decanoyl-L-glutamate
209199
Penicillium sp.
octanoate + L-glutamate
-
209199
Penicillium sp.
?
N-oleolyl-L-glutamate + H2O
-
209199
Penicillium sp.
oleate + L-glutamate
-
-
-
?
N-oleoyl-L-glutamate + H2O
67% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
oleate + L-glutamate
-
209199
Penicillium sp.
?
N-palmitoyl-L-glutamate + H2O
49% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
palmitate + L-glutamate
-
-
-
?
N-palmitoyl-L-glutamate + H2O
49% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp. B-001
palmitate + L-glutamate
-
-
-
?
N-stearoyl-L-glutamate + H2O
67% of the activity with N-decanoyl-L-glutamate
209199
Penicillium sp.
stearate + L-glutamate
-
209199
Penicillium sp.
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
pH 8.0, 15 min, stable
Penicillium sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Penicillium sp.
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
8
30°C, 5 h, stable
Penicillium sp.
Other publictions for EC 3.5.1.55
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
Synonyms
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)
209199
Murase
-
Purification and characterisat ...
Penicillium sp., Penicillium sp. B-001
Biosci. Biotechnol. Biochem.
57
854-855
1993
-
-
-
-
-
-
3
2
-
5
1
-
-
2
-
-
1
-
-
1
1
-
16
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
3
-
2
-
5
1
-
-
-
-
1
-
1
1
-
16
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
209198
Shintani
Isolation and characterization ...
Brevundimonas diminuta
J. Biochem.
96
637-643
1984
4
-
-
-
-
-
3
6
-
-
3
-
-
1
-
-
1
-
-
-
1
-
10
2
-
1
-
2
-
3
-
1
-
-
-
-
4
-
-
-
-
-
-
-
3
-
6
-
-
3
-
-
-
-
1
-
-
1
-
10
2
1
-
2
-
3
-
1
-
-
-
-
-
-
-
209197
Fukuda
A new enzyme: long acyl aminoa ...
Brevundimonas diminuta
J. Biochem.
91
1731-1738
1982
-
-
-
-
-
-
3
4
-
-
1
-
-
1
-
-
1
-
-
-
1
-
9
-
-
1
-
2
-
3
-
2
-
-
-
-
-
-
-
-
-
-
-
-
3
-
4
-
-
1
-
-
-
-
1
-
-
1
-
9
-
1
-
2
-
3
-
2
-
-
-
-
-
-
-