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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-arginase,
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D-arginine-splitting arginase
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additional information
enzyme is identical with guanidinobutyrase, EC 3.5.3.7
additional information
enzyme is identical with guanidinobutyrase, EC 3.5.3.7
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D-arginine + H2O = D-ornithine + urea
D-arginine + H2O = D-ornithine + urea
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D-arginine + H2O = D-ornithine + urea
enzyme is identical with guanidinobutyrase, EC 3.5.3.7, substrate guanidino group binding sequence
D-arginine + H2O = D-ornithine + urea
enzyme is identical with guanidinobutyrase, EC 3.5.3.7, substrate guanidino group binding sequence
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hydrolysis of linear amidines
hydrolysis of C-N bond
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hydrolysis of C-N bond
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hydrolysis of linear amidines
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hydrolysis of linear amidines
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hydrolysis of linear amidines
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D-arginine amidinohydrolase
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3-guanidinopropionate + H2O
3-aminopropanoate + urea
4-Guanidinobutyrate + H2O
4-Aminobutyrate + urea
D-arginine + H2O
D-ornithine + urea
L-arginine + H2O
L-ornithine + urea
3-guanidinopropionate + H2O
3-aminopropanoate + urea
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3-guanidinopropionate + H2O
3-aminopropanoate + urea
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4-Guanidinobutyrate + H2O
4-Aminobutyrate + urea
preferred substrate
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4-Guanidinobutyrate + H2O
4-Aminobutyrate + urea
preferred substrate
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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toad
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
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D-arginine + H2O
D-ornithine + urea
toad
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L-arginine + H2O
L-ornithine + urea
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L-arginine + H2O
L-ornithine + urea
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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D-arginine + H2O
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toad
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Zn2+
1 g-atom bound to 1 mol of subunit, dependent on, removal causes loss of activity
Co2+
can substitute for Zn2+
Mn2+
can partially substitute for Zn2+
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1,10-phenanthroline
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
5-Aminovalerate
competitive inhibition
Mercaptoacetate
strong mixed-type inhibitor
additional information
inhibition by thiol carboxylate, metal binding sequence
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additional information
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inhibition by thiol carboxylate, metal binding sequence
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additional information
additional information
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additional information
additional information
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additional information
additional information
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9
with substrate 4-guanidinobutyrate
9.5
with substrate D-arginine
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strain KUJ8602
SwissProt
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strain KUJ8602
SwissProt
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additional information
the cells can use D-arginine as sole carbon and nitrogen source
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additional information
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the cells can use D-arginine as sole carbon and nitrogen source
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additional information
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the cells can use D-arginine as sole carbon and nitrogen source
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GBH_ARTS8
Arthrobacter sp. (strain KUJ 8602)
353
0
37933
Swiss-Prot
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I3XC91_SINF2
Sinorhizobium fredii (strain USDA 257)
352
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37787
TrEMBL
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A0A021X7H5_9HYPH
323
1
34500
TrEMBL
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A0A2C9EIJ0_PSEPH
Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0)
316
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34174
TrEMBL
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A0A1Y5P9M0_9MYCO
319
0
34611
TrEMBL
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I7EI47_PHAIB
Phaeobacter inhibens (strain DSM 17395)
326
0
35353
TrEMBL
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A0A0N1FKL0_9ACTN
332
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35099
TrEMBL
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G0Q9F6_9ACTN
329
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35076
TrEMBL
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A0A2P2BYP6_9ZZZZ
321
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34620
TrEMBL
other Location (Reliability: 2)
A0A021WWA3_9HYPH
350
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37452
TrEMBL
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A0A021XBK7_9HYPH
318
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34719
TrEMBL
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A0A1U7M7G1_TISCR
355
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39553
TrEMBL
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A0A0B9A0R4_BRELN
336
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36064
TrEMBL
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A0A1J5QWB0_9ZZZZ
321
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33983
TrEMBL
other Location (Reliability: 5)
A0A0N1H0K8_9ACTN
320
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34001
TrEMBL
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A0A2N9CXX1_9BURK
318
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34355
TrEMBL
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T1XHT9_VARPD
318
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33834
TrEMBL
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A0A066PQI7_9PROT
303
0
32499
TrEMBL
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A0A0N1G9I2_9ACTN
334
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35524
TrEMBL
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A0A177HNJ1_9ACTN
334
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35468
TrEMBL
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A0A1J5SG32_9ZZZZ
315
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33737
TrEMBL
Mitochondrion (Reliability: 3)
A0A2C9EEP8_PSEPH
Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0)
318
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34231
TrEMBL
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A0A212LI87_9HYPH
uncultured Pleomorphomonas sp
300
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32111
TrEMBL
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I7DWG9_PHAIB
Phaeobacter inhibens (strain DSM 17395)
324
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35165
TrEMBL
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K9XIU1_9CHRO
326
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35307
TrEMBL
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G4I993_MYCRH
312
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33543
TrEMBL
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A0A144Y240_9BURK
316
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34177
TrEMBL
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A0A212K565_9DELT
uncultured Desulfovibrio sp
319
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34243
TrEMBL
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L7ZQT6_9BACI
321
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35759
TrEMBL
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A0A0E4A2F0_RHOER
318
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34269
TrEMBL
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A0A069RBJ7_PEPLI
316
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34776
TrEMBL
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A0A0D8FTS3_9ACTN
314
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33427
TrEMBL
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A0A1Y5PFU5_9MYCO
323
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34454
TrEMBL
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A0A1W5DH31_SERPR
310
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33689
TrEMBL
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N0CQS5_STRMI
326
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34721
TrEMBL
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A0A084G9G3_PSEDA
392
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42206
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0N0ND13_9ACTN
322
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34337
TrEMBL
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A0A0K2ASP6_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
323
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34337
TrEMBL
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A0A1J5PYN6_9ZZZZ
318
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33901
TrEMBL
Mitochondrion (Reliability: 5)
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40000
6 * 40000, SDS-PAGE
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hexamer
6 * 40000, SDS-PAGE
hexamer
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6 * 40000, SDS-PAGE
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0
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20% loss of activity in 24 h due to autolysis
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70% loss of activity in 24 h due to autolysis
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10 min, 50% loss of activity in absence of Mn2+, 10% loss of activity in presence of Mn2+
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unstable
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DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli
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Nadai, Y.
Studies on arginase. II. distribution and properties of D-arginase (D-arginine-splitting arginase)
J. Bacteriol.
45
1011-1020
1958
Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa, toad
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Arakawa, N.; Igarashi, M.; Kazuoka, T.; Oikawa, T.; Soda, K.
D-arginase of Arthrobacter sp. KUJ 8602: characterization and its identity with Zn(2+)-guanidinobutyrase
J. Biochem.
133
33-42
2003
Arthrobacter sp. (Q8KZT5), Arthrobacter sp., Arthrobacter sp. KUJ 8602 (Q8KZT5)
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