BRENDA - Enzyme Database
show all sequences of 3.5.3.10

D-arginase of Arthrobacter sp. KUJ 8602: characterization and its identity with Zn(2+)-guanidinobutyrase

Arakawa, N.; Igarashi, M.; Kazuoka, T.; Oikawa, T.; Soda, K.; J. Biochem. 133, 33-42 (2003)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli
Arthrobacter sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
Arthrobacter sp.
5-Aminovalerate
competitive inhibition
Arthrobacter sp.
Mercaptoacetate
strong mixed-type inhibitor
Arthrobacter sp.
additional information
inhibition by thiol carboxylate, metal binding sequence
Arthrobacter sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Arthrobacter sp.
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Arthrobacter sp.
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute for Zn2+
Arthrobacter sp.
Mn2+
can partially substitute for Zn2+
Arthrobacter sp.
Zn2+
1 g-atom bound to 1 mol of subunit, dependent on, removal causes loss of activity
Arthrobacter sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
6 * 40000, SDS-PAGE
Arthrobacter sp.
232000
-
gel filtration
Arthrobacter sp.
Organism
Organism
UniProt
Commentary
Textmining
Arthrobacter sp.
Q8KZT5
strain KUJ8602
-
Arthrobacter sp. KUJ 8602
Q8KZT5
strain KUJ8602
-
Purification (Commentary)
Purification (Commentary)
Organism
113fold
Arthrobacter sp.
Reaction
Reaction
Commentary
Organism
Reaction ID
D-arginine + H2O = D-ornithine + urea
enzyme is identical with guanidinobutyrase, EC 3.5.3.7, substrate guanidino group binding sequence
Arthrobacter sp.
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture-condition:L-arginine-grown cell
-
Arthrobacter sp.
-
additional information
the cells can use D-arginine as sole carbon and nitrogen source
Arthrobacter sp.
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
8.71
-
purified enzyme
Arthrobacter sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-guanidinopropionate + H2O
-
655917
Arthrobacter sp.
3-aminopropanoate + urea
-
-
-
?
3-guanidinopropionate + H2O
-
655917
Arthrobacter sp. KUJ 8602
3-aminopropanoate + urea
-
-
-
?
4-Guanidinobutyrate + H2O
preferred substrate
655917
Arthrobacter sp.
4-Aminobutyrate + urea
-
-
-
?
4-Guanidinobutyrate + H2O
preferred substrate
655917
Arthrobacter sp. KUJ 8602
4-Aminobutyrate + urea
-
-
-
?
D-arginine + H2O
-
655917
Arthrobacter sp.
D-ornithine + urea
-
-
-
?
D-arginine + H2O
-
655917
Arthrobacter sp. KUJ 8602
D-ornithine + urea
-
-
-
?
L-arginine + H2O
-
655917
Arthrobacter sp.
L-ornithine + urea
-
-
-
?
L-arginine + H2O
-
655917
Arthrobacter sp. KUJ 8602
L-ornithine + urea
-
-
-
?
Subunits
Subunits
Commentary
Organism
hexamer
6 * 40000, SDS-PAGE
Arthrobacter sp.
Synonyms
Synonyms
Commentary
Organism
More
enzyme is identical with guanidinobutyrase, EC 3.5.3.7
Arthrobacter sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Arthrobacter sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
with substrate 4-guanidinobutyrate
Arthrobacter sp.
9.5
-
with substrate D-arginine
Arthrobacter sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli
Arthrobacter sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
Arthrobacter sp.
5-Aminovalerate
competitive inhibition
Arthrobacter sp.
Mercaptoacetate
strong mixed-type inhibitor
Arthrobacter sp.
additional information
inhibition by thiol carboxylate, metal binding sequence
Arthrobacter sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Arthrobacter sp.
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Arthrobacter sp.
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute for Zn2+
Arthrobacter sp.
Mn2+
can partially substitute for Zn2+
Arthrobacter sp.
Zn2+
1 g-atom bound to 1 mol of subunit, dependent on, removal causes loss of activity
Arthrobacter sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
6 * 40000, SDS-PAGE
Arthrobacter sp.
232000
-
gel filtration
Arthrobacter sp.
Purification (Commentary) (protein specific)
Commentary
Organism
113fold
Arthrobacter sp.
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture-condition:L-arginine-grown cell
-
Arthrobacter sp.
-
additional information
the cells can use D-arginine as sole carbon and nitrogen source
Arthrobacter sp.
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
8.71
-
purified enzyme
Arthrobacter sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-guanidinopropionate + H2O
-
655917
Arthrobacter sp.
3-aminopropanoate + urea
-
-
-
?
3-guanidinopropionate + H2O
-
655917
Arthrobacter sp. KUJ 8602
3-aminopropanoate + urea
-
-
-
?
4-Guanidinobutyrate + H2O
preferred substrate
655917
Arthrobacter sp.
4-Aminobutyrate + urea
-
-
-
?
4-Guanidinobutyrate + H2O
preferred substrate
655917
Arthrobacter sp. KUJ 8602
4-Aminobutyrate + urea
-
-
-
?
D-arginine + H2O
-
655917
Arthrobacter sp.
D-ornithine + urea
-
-
-
?
D-arginine + H2O
-
655917
Arthrobacter sp. KUJ 8602
D-ornithine + urea
-
-
-
?
L-arginine + H2O
-
655917
Arthrobacter sp.
L-ornithine + urea
-
-
-
?
L-arginine + H2O
-
655917
Arthrobacter sp. KUJ 8602
L-ornithine + urea
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 40000, SDS-PAGE
Arthrobacter sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Arthrobacter sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
with substrate 4-guanidinobutyrate
Arthrobacter sp.
9.5
-
with substrate D-arginine
Arthrobacter sp.
Other publictions for EC 3.5.3.10
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)
655917
Arakawa
D-arginase of Arthrobacter sp. ...
Arthrobacter sp., Arthrobacter sp. KUJ 8602
J. Biochem.
133
33-42
2003
-
-
1
-
-
-
4
1
1
3
2
-
-
7
-
-
1
1
-
2
1
-
8
1
1
1
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
1
1
3
2
-
-
-
-
1
-
2
1
-
8
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
172136
Nadai
-
Studies on arginase. II. distr ...
Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa, toad
J. Bacteriol.
45
1011-1020
1958
-
-
-
-
-
8
9
-
-
3
-
8
-
8
-
-
-
-
-
14
-
-
16
-
-
-
-
3
-
1
1
-
-
-
-
-
-
-
-
-
-
-
8
-
9
-
-
-
3
-
8
-
-
-
-
-
14
-
-
16
-
-
-
3
-
1
1
-
-
-
-
-
-
-
-