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)

 show all sequences of 3.5.3.7

Data extracted from this reference:

Cloned(Commentary)
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
232000
-
 gel filtration Arthrobacter sp.
Organism
Organism Primary Accession No. (UniProt) Commentary Textmining
Arthrobacter sp. Q8KZT5 strain KUJ8602
-
Purification (Commentary)
Commentary Organism
113fold Arthrobacter sp.
Reaction
Reaction Commentary Organism
4-guanidinobutanoate + H2O = 4-aminobutanoate + urea enzyme is identical with D-arginase, EC 3.5.3.10, 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
3-guanidinopropionate + H2O
-
 655917 Arthrobacter sp. 3-aminopropanoate + urea
-
-
-
 ?
4-Guanidinobutyrate + H2O preferred substrate 655917 Arthrobacter sp. 4-Aminobutyrate + urea
-
-
-
 ?
D-arginine + H2O
-
 655917 Arthrobacter sp. D-ornithine + urea
-
-
-
 ?
L-arginine + H2O
-
 655917 Arthrobacter sp. L-ornithine + urea
-
-
-
 ?
Subunits
Subunits Commentary Organism
hexamer 6 * 40000, SDS-PAGE 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
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
3-guanidinopropionate + H2O
-
 655917 Arthrobacter sp. 3-aminopropanoate + urea
-
-
-
 ?
4-Guanidinobutyrate + H2O preferred substrate 655917 Arthrobacter sp. 4-Aminobutyrate + urea
-
-
-
 ?
D-arginine + H2O
-
 655917 Arthrobacter sp. D-ornithine + urea
-
-
-
 ?
L-arginine + H2O
-
 655917 Arthrobacter sp. 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.

See also following references to EC number 3.5.3.7 (sorted by year of publication):
No.1st authorPub
Med		titleorganimsjournalvolumepagesyearActivating CompoundApplicationCloned(Commentary)Crystallization (Commentary)EngineeringGeneral StabilityInhibitorsKM Value [mM]LocalizationMetals/IonsMolecular Weight [Da]Natural Substrates/ Products (Substrates)Organic Solvent StabilityOrganismOxidation StabilityPosttranslational ModificationPurification (Commentary)ReactionRenatured (Commentary)Source TissueSpecific Activity [micromol/min/mg]Storage StabilitySubstrates and Products (Substrate)SubunitsTemperature Optimum [°C]Temperature Range [°C]Temperature Stability [°C]Turnover Number [1/s]pH OptimumpH RangepH StabilityCofactorKi Value [mM]pI ValueIC50 ValueActivating 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)ExpressionGeneral InformationGeneral Information (protein specific)Expression (protein specific)KCat/KM [mM/s]KCat/KM [mM/s] (protein specific)
666275NakadaPseudomonas aeruginosa PAO1 ge ...Pseudomonas aeruginosaMicrobiology1514055-40622005--1--------1-3--------2--------------1-----------1--------2---------------
655917ArakawaD-arginase of Arthrobacter sp. ...Arthrobacter sp.J. Biochem.13333-422003--1---41131--5--11-21-411---2--------1-----4-1131----1-21-411---2---------
665366NakadaCharacterization and regulatio ...Pseudomonas aeruginosaJ. Bacteriol.1843377-33842002--1----1--21-2--1---1-31---11--------1-------1--21---1--1-31---11---------
209482YorifujiDegradation of 2-ketoarginine ...Arthrobacter globiformis, Brevibacterium helvolum, Brevibacterium linens, Pimelobacter simplex, Streptomyces griseusBiosci. Biotechnol. Biochem.59512-5131995------11---5-6--1---2-5--------------------1-1---5---1--2-5---------------
209480CampoAn arginine regulated gamma-gu ...Gallus sp., Helix pomatia, Iguania, Penicillium roqueforti, Pseudomonas fluorescens, Pseudomonas putida, Raja clavata, Streptomyces griseus, Tinca tincaArch. Int. Physiol. Biochim. Biophys.10055-601992------25-919-9--1--5-1121--1-81-------------2-5-919---1-5-1121--1-81--------
209481Yorifuji-Guanidinobutyrase for L-argini ...Arthrobacter globiformis, Brevibacterium helvolum, Brevibacterium linens, Brevibacterium lipolyticum, Corynebacterium ammoniagenes, Corynebacterium stationis, Pimelobacter simplex, Pseudomonas fluorescens, Streptomyces griseusBiosci. Biotechnol. Biochem.56773-7771992------122-139-9--1---1-132--1-1--------------12-2-139---1--1-132--1-1---------
32150Yorifuji-Distribution of amidinohydrola ...Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas sp.Agric. Biol. Chem.472825-283019832----------4-4--4---2-41-----------2-------------4---4--2-41--------------
209442YorifujiTaurocyamine-utilizing mutants ...Pseudomonas fluorescensJ. Appl. Biochem.5375-38119831----------1-4--1-----2------------1-------------1---1----2---------------
32148Yorifuji-Characterization of 3-guanidin ...Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas sp.Agric. Biol. Chem.461361-136719828--1--4--333-4--3-----31----2------8---1---4---333---3----31----2---------
209439Yorifuji-Gratuitous induction of two om ...Pseudomonas fluorescens, Pseudomonas sp.Agric. Biol. Chem.46317-31819823----------2-2--------3------------3-------------2--------3---------------
209476Yorifuji-4-Guanidinobutyrate amidinohyd ...Flavobacterium sp., Pseudomonas fluorescens, Pseudomonas sp.Agric. Biol. Chem.441127-11341980---1-161-233-3--3---1-81--1-1-1--------1-1-6-1-233---3--1-81--1-1-1-------
32149Yorifuji-3-Guanidinopropionate amidinoh ...Pseudomonas aeruginosa, Pseudomonas fluorescens, Raja clavataAgric. Biol. Chem.421789-17901978-----------3-4--2---114--------------------------3---2--114---------------
209474ChouMetabolism of basic amino acid ...Gallus sp., Helix pomatia, Iguania, Penicillium roqueforti, Pseudomonas fluorescens, Pseudomonas putida, Raja clavata, Streptomyces griseusJ. Biol. Chem.2474486-44901972-------61838-8--6--58114-2---111---------------61838---6-58114-2---111--------
209473Van ThoaiInduction et specificite des e ...Streptomyces griseusBiochim. Biophys. Acta11573-801966-----------1-1--1-----2--------------------------1---1----2---------------
209472MoraCharacteristics of arginases f ...Ambystoma mexicanum, Crotalus sp., Gallus sp., Gopherus sp., Iguania, Kinosternon sp., no activity in Neurospora crassa, Pseudemys sp., Rana sp., Streptomyces griseusBiochem. J.96588-5941965---------319-11--1--4--10-----3------------------319---1-4--10-----3---------