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Ligand L-citrulline

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

arginine metabolism, urea cycle

KEGG

Arginine biosynthesis, Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Biosynthesis of various secondary metabolites - part 3

MetaCyc

L-arginine biosynthesis I (via L-ornithine), L-arginine biosynthesis II (acetyl cycle), L-arginine biosynthesis III (via N-acetyl-L-citrulline), L-arginine biosynthesis IV (archaea), L-arginine degradation V (arginine deiminase pathway), L-arginine degradation XIII (reductive Stickland reaction), L-arginine degradation XIV (oxidative Stickland reaction), L-citrulline biosynthesis, L-citrulline degradation, nitric oxide biosynthesis I (plants), nitric oxide biosynthesis II (mammals), nitric oxide biosynthesis III (bacteria), urea cycle more

Show all BRENDA pathways known for L-citrulline

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Natural Substrate (22 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.20

L-citrulline + H2O = ?

171972, 171968, 171967, 171969

-

3.5.1.20

L-citrulline + H2O = L-ornithine + CO2 + NH3

753986

-

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

662377, 662205, 661285, 662254

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

662377, 662205, 661285, 662254

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

662377, 662205, 661285, 662254

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

662377, 662205, 661285, 662254

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

662377, 662205, 661285, 662254

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692659, 725629, 728544, 690765, 690234, 693030, 692607, 690727, 690768, 749045

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692659, 725629, 728544, 690765, 690234, 693030, 692607, 690727, 690768, 749045

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692659, 725629, 728544, 690765, 690234, 693030, 692607, 690727, 690768, 749045

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692659, 725629, 728544, 690765, 690234, 693030, 692607, 690727, 690768, 749045

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692659, 725629, 728544, 690765, 690234, 693030, 692607, 690727, 690768, 749045

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

651195, 652231, 652242, 652404, 650761

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

651195, 652231, 652242, 652404, 650761

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

651195, 652231, 652242, 652404, 650761

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

651195, 652231, 652242, 652404, 650761

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

651195, 652231, 652242, 652404, 650761

2nz2, 3D-view

3.5.1.20

2 entries

6.3.4.5

20 entries

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

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Show Natural Product (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.3

carbamoyl phosphate + L-ornithine = L-citrulline + phosphate

-

4jqo, 3D-view

2.1.3.3

carbamoyl phosphate + L-ornithine = phosphate + L-citrulline

, 485904, 485901, 485898, 485895, 485922, 485925, 485918

4jqo, 3D-view

2.1.3.3

2 entries

2.1.3.6

carbamoyl phosphate + L-ornithine = phosphate + N-carbamoyl-L-ornithine

-

-

3.5.1.B4

N2-acetyl-L-citrulline + H2O = L-citrulline + acetate

-

-

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

1h70, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2c6z, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2jai, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

1h70, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2c6z, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2jai, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

1h70, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2c6z, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2jai, 3D-view

3.5.3.18

9 entries

3.5.3.6

L-arginine + H2O = L-citrulline + NH3

-

1lxy, 3D-view

Substrate in Enzyme-catalyzed Reactions (62 results)

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Show Substrate (62 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.2

L-citrulline + H2O + O2 = 2-oxo-5-ureidovaleric acid + NH3 + H2O2

711874

-

1.4.3.2

L-citrulline + H2O + O2 = ?

391785

-

1.4.3.2

L-citrulline + H2O + O2 = ? + NH3 + H2O2

651026

-

1.4.3.2

L-citrulline + H2O + O2 = N-carbamoyl-5-amino-2-oxopentanoic acid + NH3 + H2O2

651026

-

1.4.3.2

4 entries

1.5.1.11

L-Citrulline + pyruvate + NADPH = N2-(D-1-Carboxyethyl)-L-citrulline + NADP+ + H2O

13323

-

1.5.1.16

L-citrulline + pyruvate + NADH + H+ = ?

392094

-

2.1.3.3

arsenate + L-citrulline = carbamoylarsenate + L-ornithine

485938

4jqo, 3D-view

2.1.3.3

phosphate + L-citrulline = carbamoyl phosphate + L-ornithine

701115

4jqo, 3D-view

2.1.3.3

phosphate + L-citrulline = carbamoylphosphate + L-ornithine

666005, 664807

4jqo, 3D-view

2.1.3.3

3 entries

2.6.1.28

phenylpyruvate + L-citrulline = phenylalanine + 2-oxo-5-ureido-pentanoate

639949

-

3.4.11.17

L-citrulline + H2O = (2S)-2-amino-5-(carboxyamino)pentanoic acid + NH3

665098

-

3.5.1.20

L-citrulline + H2O = ?

171972, 171968, 171967, 171969

-

3.5.1.20

L-citrulline + H2O = L-ornithine + CO2 + NH3

753986

-

3.5.1.57

L-citrullin + H2O = ?

81203

-

3.5.1.57

L-citrulline + H2O = ?

668755

-

3.5.1.20

2 entries

3.5.1.57

2 entries

3.5.1.6

N-carbamoyl-L-ornithine + H2O = L-ornithine + CO2 + NH3

720104

-

4.1.1.64

2-Oxobutanoate + L-citrulline = ?

4748

-

5.1.1.10

L-Citrulline = D-Citrulline

2047, 2045, 2041

-

5.1.1.9

L-Citrulline = D-Citrulline

2166, 2165

-

6.1.1.19

ATP + L-citrulline + tRNACCCG = AMP + diphosphate + L-citryl-tRNACCCG

726863

-

6.3.4.5

ATP + L-citrulline + 3-nitro-2-aminopropanoate = ?

1587

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + 3-nitro-2-aminopropanoate = ?

1587

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + 3-nitro-2-aminopropanoate = ?

1587

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + 3-nitro-2-aminopropanoate = ?

1587

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + 3-nitro-2-aminopropanoate = ?

1587

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = ?

1594, 1591, 1579, 1598

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

1593, 1578, 1581, 1583, 1584, 1586, 1595, 1598, 1575, 1580, 1582, 1591, 1592, 1594, 1597, 1596, 1577, 1585, 1587, 1588, 1589, 1573, 1590, 1576, 1579, 1574, 662377, 662205, 661285, 662254

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

1593, 1578, 1581, 1583, 1584, 1586, 1595, 1598, 1575, 1580, 1582, 1591, 1592, 1594, 1597, 1596, 1577, 1585, 1587, 1588, 1589, 1573, 1590, 1576, 1579, 1574, 662377, 662205, 661285, 662254

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

1593, 1578, 1581, 1583, 1584, 1586, 1595, 1598, 1575, 1580, 1582, 1591, 1592, 1594, 1597, 1596, 1577, 1585, 1587, 1588, 1589, 1573, 1590, 1576, 1579, 1574, 662377, 662205, 661285, 662254

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

1593, 1578, 1581, 1583, 1584, 1586, 1595, 1598, 1575, 1580, 1582, 1591, 1592, 1594, 1597, 1596, 1577, 1585, 1587, 1588, 1589, 1573, 1590, 1576, 1579, 1574, 662377, 662205, 661285, 662254

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-Asp = AMP + diphosphate + L-argininosuccinate

1593, 1578, 1581, 1583, 1584, 1586, 1595, 1598, 1575, 1580, 1582, 1591, 1592, 1594, 1597, 1596, 1577, 1585, 1587, 1588, 1589, 1573, 1590, 1576, 1579, 1574, 662377, 662205, 661285, 662254

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692607, 690768, 692659, 690727, 690765, 725629, 693030, 728544, 749045, 690234

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692607, 690768, 692659, 690727, 690765, 725629, 693030, 728544, 749045, 690234

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692607, 690768, 692659, 690727, 690765, 725629, 693030, 728544, 749045, 690234

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692607, 690768, 692659, 690727, 690765, 725629, 693030, 728544, 749045, 690234

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate

692607, 690768, 692659, 690727, 690765, 725629, 693030, 728544, 749045, 690234

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

675096, 652976, 651195, 653344, 676636, 652231, 652404, 652242, 649104, 650761

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

675096, 652976, 651195, 653344, 676636, 652231, 652404, 652242, 649104, 650761

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

675096, 652976, 651195, 653344, 676636, 652231, 652404, 652242, 649104, 650761

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

675096, 652976, 651195, 653344, 676636, 652231, 652404, 652242, 649104, 650761

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate

675096, 652976, 651195, 653344, 676636, 652231, 652404, 652242, 649104, 650761

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-hydroxy-DL-Asp = ?

1574

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-hydroxy-DL-Asp = ?

1574

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-hydroxy-DL-Asp = ?

1574

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-hydroxy-DL-Asp = ?

1574

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-hydroxy-DL-Asp = ?

1574

2nz2, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-methyl-L-Asp = ?

1574

1j1z, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-methyl-L-Asp = ?

1574

1j21, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-methyl-L-Asp = ?

1574

1k97, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-methyl-L-Asp = ?

1574

1kp3, 3D-view

6.3.4.5

ATP + L-citrulline + threo-beta-methyl-L-Asp = ?

1574

2nz2, 3D-view

6.3.4.5

dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate

1576

1j1z, 3D-view

6.3.4.5

dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate

1576

1j21, 3D-view

6.3.4.5

dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate

1576

1k97, 3D-view

6.3.4.5

dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate

1576

1kp3, 3D-view

6.3.4.5

dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate

1576

2nz2, 3D-view

7.4.2.1

ATP + H2O + citrulline/out = ADP + phosphate + citrulline/in

700356, 720414

-

7.4.2.1

ATP + H2O + L-citrulline/out = ADP + phosphate + L-citrulline/in

686013

-

6.3.4.5

40 entries

7.4.2.1

2 entries

Product in Enzyme-catalyzed Reactions (66 results)

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Show Product (66 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.39

Nomega-hydroxy-L-arginine + NADPH + H+ + O2 = L-citrulline + NADP+ + NO + H2O

-

-

2.1.3.3

carbamoyl phosphate + L-ornithine = L-citrulline + phosphate

-

4jqo, 3D-view

2.1.3.3

carbamoyl phosphate + L-ornithine = phosphate + L-citrulline

485911, 485894, 485919, 485900, 485921, 485935, 485934, 485920, , 485898, 485926, 485927, 485933, 485902, 485912, 485914, 485917, 485923, 485928, 485899, 485925, 485890, 485892, 485909, 485924, 485893, 485918, 485946, 485903, 485906, 485910, 485932, 485908, 485915, 485922, 485916, 485907, 485904, 485957, 485901, 485905, 485897, 485896, 485945, 485895, 485913, 485891, 209399, 485929, 485930, 485889

4jqo, 3D-view

2.1.3.3

2 entries

2.1.3.6

carbamoyl phosphate + L-ornithine = phosphate + N-carbamoyl-L-ornithine

-

-

3.5.1.B4

N2-acetyl-L-citrulline + H2O = L-citrulline + acetate

-

-

3.5.3.15

L-Arg + H2O = L-citrulline + NH3

-

-

3.5.3.15

L-arginine + H2O = L-citrulline + NH3

-

-

3.5.3.15

L-arginine-methyl ester + H2O = L-citrulline + NH3

-

-

3.5.3.18

dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

1h70, 3D-view

3.5.3.18

dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2c6z, 3D-view

3.5.3.18

dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2jai, 3D-view

3.5.3.18

N,N-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 652188

1h70, 3D-view

3.5.3.18

N,N-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 652188

2c6z, 3D-view

3.5.3.18

N,N-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 652188

2jai, 3D-view

3.5.3.18

N-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

1h70, 3D-view

3.5.3.18

N-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2c6z, 3D-view

3.5.3.18

N-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2jai, 3D-view

3.5.3.18

N5-(methoxycarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

1h70, 3D-view

3.5.3.18

N5-(methoxycarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

2c6z, 3D-view

3.5.3.18

N5-(methoxycarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

2jai, 3D-view

3.5.3.18

N5-(methylcarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

1h70, 3D-view

3.5.3.18

N5-(methylcarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

2c6z, 3D-view

3.5.3.18

N5-(methylcarbamimidoyl)-L-ornithine + H2O = L-citrulline + ?

-

2jai, 3D-view

3.5.3.18

N5-[2,5-dihydro-1H-pyrrol-1-yl(imino)methyl]-L-ornithine + H2O = L-citrulline + ?

-

1h70, 3D-view

3.5.3.18

N5-[2,5-dihydro-1H-pyrrol-1-yl(imino)methyl]-L-ornithine + H2O = L-citrulline + ?

-

2c6z, 3D-view

3.5.3.18

N5-[2,5-dihydro-1H-pyrrol-1-yl(imino)methyl]-L-ornithine + H2O = L-citrulline + ?

-

2jai, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 288971

1h70, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 288971

2c6z, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

, 288971

2jai, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

1h70, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2c6z, 3D-view

3.5.3.18

NG,NG-dimethyl-L-arginine + H2O = L-citrulline + dimethylamine

-

2jai, 3D-view

3.5.3.18

NG-methyl arginine + H2O = L-citrulline + methylamine

-

1h70, 3D-view

3.5.3.18

NG-methyl arginine + H2O = L-citrulline + methylamine

-

2c6z, 3D-view

3.5.3.18

NG-methyl arginine + H2O = L-citrulline + methylamine

-

2jai, 3D-view

3.5.3.18

NG-methyl-L-arginine + H2O = L-citrulline + methylamine

-

1h70, 3D-view

3.5.3.18

NG-methyl-L-arginine + H2O = L-citrulline + methylamine

-

2c6z, 3D-view

3.5.3.18

NG-methyl-L-arginine + H2O = L-citrulline + methylamine

-

2jai, 3D-view

3.5.3.18

Ngamma-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

1h70, 3D-view

3.5.3.18

Ngamma-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2c6z, 3D-view

3.5.3.18

Ngamma-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2jai, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

1h70, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2c6z, 3D-view

3.5.3.18

Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2jai, 3D-view

3.5.3.18

Nomega,Nomega-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

1h70, 3D-view

3.5.3.18

Nomega,Nomega-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2c6z, 3D-view

3.5.3.18

Nomega,Nomega-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

-

2jai, 3D-view

3.5.3.18

Nomega-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

1h70, 3D-view

3.5.3.18

Nomega-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2c6z, 3D-view

3.5.3.18

Nomega-monomethyl-L-arginine + H2O = L-citrulline + methylamine

-

2jai, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = L-citrulline + methanethiol

-

1h70, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = L-citrulline + methanethiol

-

2c6z, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = L-citrulline + methanethiol

-

2jai, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = methanethiol + L-citrulline

-

1h70, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = methanethiol + L-citrulline

-

2c6z, 3D-view

3.5.3.18

S-methyl-L-thiocitrulline + H2O = methanethiol + L-citrulline

-

2jai, 3D-view

3.5.3.6

L-Arg + H2O = L-citrulline + NH3

209455, 209469, 209446, 209447, 209454, 209466, 209465, 209464, 209468, 209463, 209456, 209457, 209459, 209448, 209458, 209461, 209462, 209467, 209470, 209471, 209449, 209450, 209451, 209452, 209453, , 209460

1lxy, 3D-view

3.5.3.6

L-arginine + H2O = L-citrulline + NH3

, 651600

1lxy, 3D-view

3.5.3.6

Nomega-amino-Arg + H2O = L-citrulline + hydrazine

-

1lxy, 3D-view

3.5.3.6

Nomega-amino-L-arginine + H2O = hydrazine + L-citrulline

-

1lxy, 3D-view

3.5.3.6

Nomega-amino-L-arginine + H2O = L-citrulline + hydrazine

-

1lxy, 3D-view

3.5.3.6

Nomega-methyl-Arg + H2O = L-citrulline + methylamine

-

1lxy, 3D-view

3.5.3.6

Nomega-methyl-L-arginine + H2O = L-citrulline + methylamine

-

1lxy, 3D-view

7.4.2.1

ATP + H2O + citrulline/out = ADP + phosphate + citrulline/in

-

-

7.4.2.1

ATP + H2O + L-citrulline/out = ADP + phosphate + L-citrulline/in

-

-

7.4.2.1

ATP + H2O + L-citrulline-[L-citrulline-binding protein][side 1] = ADP + phosphate + L-citrulline[side 2] + [L-citrulline-binding protein][side 1]

-

-

3.5.3.15

3 entries

3.5.3.18

48 entries

3.5.3.6

7 entries

7.4.2.1

3 entries

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.2

pH 7.6, 30°C

651026

-

2.3.1.1

10 mM, 75% inhibition

486063

-

2.3.1.35

-

736594

-

2.7.2.2

-

735216

-

2.7.2.8

-

642353, 642356

-

3.5.3.18

-

670913, 711211

1h70, 3D-view

3.5.3.18

-

670913, 711211

2c6z, 3D-view

3.5.3.18

-

670913, 711211

2jai, 3D-view

3.5.3.18

competitive

288971

1h70, 3D-view

3.5.3.18

competitive

288971

2c6z, 3D-view

3.5.3.18

competitive

288971

2jai, 3D-view

3.5.3.18

6 entries

3.5.3.6

-

209455

1lxy, 3D-view

7.4.2.1

1% cell growth, 1% viability of cells

675890

-

3D Structure of Enzyme-Ligand-Complex (PDB) (99 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (99 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.1.3.3

4jqo, 3D-view

2.7.1.37

1ol1, 3D-view

2.7.3.3

4gvy, 3D-view

3.2.1.17

3oe0, 3D-view

3.4.21.36

1qr3, 3D-view

3.4.21.75

6eqv, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

1h70, 3D-view

3.5.3.18

2c6z, 3D-view

3.5.3.18

2jai, 3D-view

3.5.3.18

27 entries

3.5.3.6

1lxy, 3D-view

4.2.1.11

5nig, 3D-view

5.2.1.8

6o34, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

3zop, 3D-view

5.4.99.5

3zp7, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

6.3.4.5

1j1z, 3D-view

6.3.4.5

1j21, 3D-view

6.3.4.5

1k97, 3D-view

6.3.4.5

1kp3, 3D-view

6.3.4.5

2nz2, 3D-view

5.4.99.5

18 entries

6.3.4.5

45 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.1.3.3

8.1

-

pH 8.0, 37°C

701115

2.1.3.3

90

-

-

485891

2.1.3.3

2 entries

3.5.1.6

0.08

-

pH 8.0, 30°C

720104

K_M Value (9 results)

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Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.2

0.026

-

pH 7.6, 30°C

651026

1.4.3.2

21.3

-

fraction II

391785

1.5.1.11

22

-

L-Met, with pyruvate and NADPH as cosubstrate

13323

1.5.1.11

22

-

with pyruvate and NADPH as cosubstrates

13323

1.4.3.2

2 entries

1.5.1.11

2 entries

1.5.1.16

17.1

-

-

392094

2.1.3.3

10.4

-

pH 8.0, 37°C

701115

3.5.1.6

9.47

-

pH 8.0, 30°C

720104

6.3.4.5

0.026

-

enzyme form ASSI

1582

6.3.4.5

0.03

-

normal liver

1578

6.3.4.5

2 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.2

20.6

-

pH 7.6, 30°C

651026

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.3.1.35

30

-

pH 7.5, 37°C

736594

3.5.3.18

3.7

-

pH 7.3, temperature not specified in the publication

711211

References & Links

Literature References (166)

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Show Reference (166 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1573

-

Purification of argininosuccinate synthetase from cotyledons of germinating peas

1971

Shargool, P.D.

Phytochemistry

10

2029-2032

1574

4355767

Enzymes of arginine and urea synthesis

1973

Ratner, S.

Adv. Enzymol. Relat. Areas Mol. Biol.

39

1-90

1575

5300

Crystallization and some properties of argininosuccinate synthetase from rat liver

1975

Saheki, T.; Kusumi, T.; Takada, S.; Katsunuma, T.; Katunuma, N.

FEBS Lett.

58

314-317

1576

405380

Studies of rat liver argininosuccinate synthetase. I. Physicochemical, catalytic, and immunochemical properties

1977

Saheki, T.; Kusumi, T.; Takada, S.; Katsunuma, T.

J. Biochem.

81

687-696

1577

885853

Biosynthesis of urea. Molecular and regulatory properties of crystalline argininosuccinate synthetase

1977

Rochovansky, O.; Kodowaki, H.; Ratner, S.

J. Biol. Chem.

252

5287-5294

1578

762042

Studies on liver argininosuccinate synthetase in a patient with citrullinemia and in normal subjects

1979

Matsuda, Y.; Tsuji, A.; Katunuma, N.; Hayashi, M.; Takahashi, Y.

J. Biochem.

85

191-195

1579

35347

Yeast argininosuccinate synthetase. Purification, structural and kinetic properties

1979

Hilger, F.; Simon, J.P.; Stalon, V.

Eur. J. Biochem.

94

153-163

1580

447618

Studies on rat liver argininosuccinate synthetase. Inhibition by various amino acids

1979

Takada, S.; Saheki, T.; Igarashi, Y.; Katsunuma, T.

J. Biochem.

85

1309-1314

1581

518841

Isolation and characterization of argininosuccinate synthetase from human liver

1979

O'Brien, W.E.

Biochemistry

18

5353-5356

1582

118168

Studies of rat liver argininosuccinate synthetase. The presence of three forms, and their physicochemical, catalytic, and immunochemical properties

1979

Takada, S.; Kusumi, T.; Saheki, T.; Tsuda, M.; Katsunuma, T.

J. Biochem.

86

1353-1359

1583

6766737

Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts

1980

Kimball, M.E.; Jacoby, L.B.

Biochemistry

19

705-709

1584

7446299

Role of argininosuccinate synthetase in the regulation of urea synthesis in the rat and argininosuccinate synthetase-associated metabolic disorder in man

1986

Saheki, T.; Tsuda, M.; Takada, S.; Kusumi, K.; Katsunuma, T.

Adv. Enzyme Regul.

18

221-238

1585

6957859

Argininosuccinate synthetase of bovine liver: chemical and physical properties

1982

Ratner, S.

Proc. Natl. Acad. Sci. USA

79

5197-5199

1586

6885737

Some properties of argininosuccinate synthetase purified from human liver and a comparison with the rat liver enzyme

1983

Saheki, T.; Sase, M.; Nakano, K.; Azuma, F.; Katsunuma, T.

J. Biochem.

93

1531-1537

1587

6605113

Kinetic mechanism of argininosuccinate synthetase

1983

Raushell, F.M.; Seiglie, J.L.

Arch. Biochem. Biophys.

225

979-985

1588

6547814

Nitro analogs of substrates for argininosuccinate synthetase and argininosuccinate lyase

1984

Raushel, F.M.

Arch. Biochem. Biophys.

232

520-525

1589

3863125

Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation

1985

Kumar, S.; Lennane, J.; Ratner, S.

Proc. Natl. Acad. Sci. USA

82

6745-6749

1590

9477156

Distribution and co-localization of nitric oxide synthetase and argininosuccinate synthetase in the cat hypothalamus

1997

Isayama, H.; Nakamura, H.; Kanemura, H.; Kobayashi, K.; Emson, P.C.; Kawabuchi, M.; Tashiro, N.

Arch. Histol. Cytol.

60

477-492

1591

7776957

Regulation of argininosuccinate synthetase level by corticosteroid and pancreatic hormones during perinatal period

1995

Demarquoy, J.; Fairand, A.; Gautier, C.; Vaillant, T.

Mol. Cell. Biochem.

143

47-51

1592

7845368

Demonstration of argininosuccinate synthetase activity associated with mitochondrial membrane: characterization and hormonal regulation

1994

Demarquoy, J.; Fairand, A.; Gautier, C.; Vaillant, R.

Mol. Cell. Biochem.

136

145-155

1593

8197477

Generation of a mouse model for citrullinemia by targeted disruption of the argininosuccinate synthetase gene

1994

Patejunas, G.; Bradley, A.; Beaudet, A.L.; O'Brien, W.E.

Somat. Cell Mol. Genet.

20

55-60

1594

1283210

Immunohistochemical localization of argininosuccinate synthetase in the rat brain in relation to nitric oxide synthase-containg neurons

1992

Arnt-Ramos, L.R.; O'Brien, W.E.; Vincent, S.R.

Neuroscience

51

773-789

1595

2788888

Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase

1989

Isahiki, Y.; Noda, T.; Kobayashi, K.; Sase, M.; Saheki, T.; Titani, K.

Protein Seq. Data Anal.

2

283-287

1596

1372742

Renal argininosuccinate synthetase: purification, immunohistochemical localization, and elastin-binding property

1992

Wakui, H.; Komatsuda, A.; Itoh, H.; Kobayashi, R.; Nakamoto, Y.; Miura, A.B.

Renal Physiol. Biochem.

15

1-9

1597

8586639

Preparation of recombinant argininosuccinate synthetase and arguininosuccinate lyase: expression of the enzymes in rat tissues

1995

Yu, Y.; Terada, K.; Nagasaki, A.; Takiguchi, M.; Mori, M.

J. Biochem.

117

952-957

1598

8792870

Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells

1994

Shaheen, N.; Kobayashi, K.; Terazono, H.; Fukushige, T.; Horiuchi, M.; Saheki, T.

Enzyme Protein

95

251-264

2041

-

Amino acid racemase (Pseudomonas striata)

1971

Soda, K.; Osumi, T.

Methods Enzymol.

17

629-636

2045

-

Purification and characterization of amino acid racemase with very broad substrate specificity from Aeromonas caviae

1987

Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

51

173-180

2047

8320235

A new amino acid racemase with threonine alpha-epimerase activity from Pseudomonas putida: purification and characterization

1993

Lim, Y.H.; Yokoigawa, K.; Esaki, N.; Soda, K.

J. Bacteriol.

175

4213-4217

2165

-

Arginine racemase (Pseudomonas graveolens)

1976

Soda, K.; Yorifuji, T.; Ogata, K.

Methods Enzymol.

17A

341-345

2166

5570439

Arginine racemase of Pseudomonas graveolens. I. Purification, crystallization, and properties

1971

Yorifuji, T.; Ogata, K.

J. Biol. Chem.

246

5085-5092

4748

-

L-Alanine-alpha-ketobutyrate aminotransferase of Pseudomonas sp.

1981

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

45

775-776

13323

-

Octopine dehydrogenase of a Vinca rosea crown gall-tumor

1983

Birnberg, P.R.; Rao, S.S.; Lippincott, J.A.

Phytochemistry

22

1345-1355

81203

-

Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum

1983

Iwayama, A.; Kimura, T.; Adachi, O.; Ameyama, M.

Agric. Biol. Chem.

47

2483-2493

171967

-

Enzymes of ornithine-arginine metabolism in trypanosomatids of the genus Phytomonas

1987

Camargo Plessmann, E.; Silva, S.; Roitmann, I.; De Souza, W.; Jankevicius, J.V.; Dollet, M.

J. Protozool.

34

439-441

171968

-

L-Citrulline

1985

Eichler, W.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

8

412-418

171969

-

Subcellular distribution and some properties of citrullinase in Euglena gracilis Z

1985

Park, B.S.; Hirotani, A.; Nakano, Y.; Kitaoka, S.

Agric. Biol. Chem.

49

2205-2206

171972

2340108

Regulation of growth and polyamine biosynthesis of the ciliated protozoan Tetrahymena thermophila. Effects of L-arginine metabolites and polyamines

1990

Eichler, W.

Biol. Chem. Hoppe-Seyler

371

273-282

209399

6895223

Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)

1981

Srivenugopal, K.S.; Adiga, P.R.

J. Biol. Chem.

256

9532-9541

209446

237904

Crystallization and properties of L-arginine deiminase of Pseudomonas putida

1975

Shibatani, T.; Kakimoto, T.; Chibata, I.

J. Biol. Chem.

250

4580-4583

209447

11946203

Crystallization of L-arginine-deiminase from Pseudomonas putida

1971

Kakimoto, T.; Shibatani, T.; Chibata, I.

FEBS Lett.

19

166-168

209448

1262306

Role of arginine deiminase in growth of Mycoplasma hominis

1976

Fenske, J.D.; Kenny, G.E.

J. Bacteriol.

126

501-510

209449

856796

Arginine deiminase from Mycoplasma arthritidis. Evidence for multiple forms

1977

Weickmann, J.L.; Fahrney, D.E.

J. Biol. Chem.

252

2615-2620

209450

697801

Catalysis by arginine deiminase: evidence for a covalent intermediate

1978

Smith, D.W.; Fahrney, D.E.

Biochem. Biophys. Res. Commun.

83

101-106

209451

697802

Arginine deiminase: demonstration of two active sites and possible half-of-the-sites reactivity

1978

Weickmann, J.L.; Himmel, M.E.; Smith, D.W.; Fahrney, D.E.

Biochem. Biophys. Res. Commun.

83

107-113

209452

681335

Arginine deiminase from Mycoplasma arthritidis. Properties of the enzyme from log phase cultures

1978

Weickmann, J.L.; Himmel, M.E.; Squire, P.G.; Fahrney, D.E.

J. Biol. Chem.

253

6010-6015

209453

681336

Arginine deiminase from Mycoplasma arthritidis. Structure-activity relationships among substrates and competitive inhibitors

1978

Smith, D.W.; Ganaway, R.L.; Fahrney, D.E.

J. Biol. Chem.

253

6016-6020

209454

729806

Subunit and amino acid composition of L-arginine deiminase of Pseudomonas putida

1978

Shibatani, T.; Kakimoto, T.; Chibata, I.

FEBS Lett.

96

389-391

209455

-

Purification and some properties of arginine deiminase in Euglena gracilis Z

1984

Park, B.S.; Hirotani, A.; Nakano, Y.; Kitaoka, S.

Agric. Biol. Chem.

48

483-489

209456

-

Isolation and properties of arginine deiminase in Lactobacillus buchneri NCDO110

1984

Manca de Nadra, M.C.; Pesce de Ruiz Holgado, A.A.; Oliver, G.

J. Appl. Biochem.

6

184-187

209457

2866109

Increased formation of arginine deiminase by Clostridium perfringens FD-1 growing in the presence of caffeine

1984

Sacks, L.E.

Experientia

41

1435-1437

209458

3806049

Arginine deiminase of Mycoplasma hominis: cytoplasmic and membrane-associated forms

1986

Lin, J.S.L.

J. Gen. Microbiol.

132

1467-1474

209459

-

Intracellular localization of the arginine deiminase pathway in Streptococcus mitis

1987

Hiraoka, B.Y.; Harada, M.; Fukasawa, K.; Mogi, M.

Curr. Microbiol.

15

81-84

209460

9468500

Cloning and expression of a prokaryotic enzyme, arginine deiminase, from primitive eukaryote Giardia intestinalis

1998

Knodler, L.A.; Sekyere, E.O.; Stewart, T.S.; Schofield, P.J.; Edwards, M.R.

J. Biol. Chem.

273

4470-4477

209461

9071817

Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase

1997

Komada, Y.; Zhang, X.L.; Zhou, Y.W.; Ido, M.; Azuma, E.

Int. J. Hematol.

65

129-141

209462

10901172

Cytoprotective effect of arginine deiminase on taxol-induced apoptosis in DU145 human prostate cancer cells

2000

Kang, S.W.; Kang, H.; Park, I.S.; Choi, S.H.; Shin, K.H.; Chun, Y.S.; Chun, G.B.; Min, B.H.

Mol. Cells

10

331-337

209463

16534912

Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic acid bacteria

1995

Liu, S.Q.; Pritchard, G.G.; Hardman, M.J.; Pilone, G.J.

Appl. Environ. Microbiol.

61

310-316

209464

8813682

The contribution of the arginine dihydrolase pathway to energy metabolism by Trichomonas vaginalis

1996

Yarlett, N.; Martinez, M.P.; Moharrami, M.A.; Tachezy, J.

Mol. Biochem. Parasitol.

78

117-125

209465

-

Arginine deiminase from Halobacterium salinarium. Purification and properties

1990

Monstadt, G.M.; Holldorf, A.W.

Biochem. J.

273

739-745

209466

1568792

In vivo anti-tumor activity of arginine deiminase purified from Mycoplasma arginini

1992

Takaku, H.; Takase, M.; Abe, S.i.; Hayashi, H.; Miyazaki, K.

Int. J. Cancer

51

244-249

209467

2370103

Identification and purification of arginine deiminase that originated from Mycoplasma arginini

1990

Sugimura, K.; Fukuda, S.; Wada, Y.; Taniai, M.; Suzuki, M.; Kimura, T.; Ohno, T.; Yamamoto, K.; Azuma, I.

Infect. Immun.

58

2510-2515

209468

9632565

Inhibition of human peripheral blood mononuclear cell proliferation by Streptococcus pyogenes cell extract is associated with arginine deiminase activity

1998

Degnan, B.A.; Palmer, J.M.; Robson, T.; Jones, C.E.D.; Fischer, M.; Glanville, M.; Mellor, G.D.; Diamond, A.G.; Kehoe, M.A.; Goodacre, J.A.

Infect. Immun.

66

3050-3058

209469

2228433

The arginine dihydrolase pathway is present in Giardia intestinalis

1990

Schofield, P.J.; Costello, M.; Edwards, M.R.; OæSullivan, W.J.

Int. J. Parasitol.

20

697-699

209470

7765234

High-level expression of Mycoplasma arginine deiminase in Escherichia coli and its efficient renaturation as an anti-tumor enzyme

1994

Misawa, S.; Aoshima, M.; Takaku, H.; Matsumoto, M.; Hayashi, H.

J. Biotechnol.

36

145-155

209471

10803513

Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis

2000

Gong, H.; Zoelzer, F.; von Recklinghausen, G.; Havers, W.; Schweigerer, L.

Leukemia

14

826-829

288971

2722865

Purification and properties of a new enzyme, NG,NG-dimethylarginine dimethylaminohydrolase from rat kidney

1989

Ogawa, T.; Kimoto, M.; Sasaoka, K.

J. Biol. Chem.

264

10205-10209

391785

234421

L-amino acid oxidases of Proteus rettgeri

1975

Duerre, J.A.; Chakrabarty, S.

J. Bacteriol.

121

656-663

392094

21695

Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue

1977

Otten, L.A.B.M.; Vreugdenhil, D.; Schilperoort, R.A.

Biochim. Biophys. Acta

485

268-277

485889

6034676

Crystalline ornithine transcarbamylase

1967

Bishop, S.H.; Grisolia, S.

Biochim. Biophys. Acta

139

344-348

485890

4622303

Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure

1972

Marshall, M.; Cohen, P.P.

J. Biol. Chem.

247

1641-1653

485891

4622304

Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics

1972

Marshall, M.; Cohen, P.P.

J. Biol. Chem.

247

1654-1668

485892

4622305

Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity

1972

Marshall, M.; Cohen, P.P.

J. Biol. Chem.

247

1669-1682

485893

3566963

Ornithine transcarbamylase from Mycobacterium smegmatis ATCC 14468: purification, properties, and reaction mechanism

1986

Ahmad, S.; Bhatnagar, R.K.; Venkitasubramanian, T.A.

Biochem. Cell Biol.

64

1349-1355

485894

-

Some characteristics of hepatic ornithine transcarbamylase from the house musk shrew, Suncus murinus

1985

Tsuji, S.; Kanazawa, S.; Fukushina, T.; Oda, S.

Nippon Chikusan Gakkai Ho

56

962-970

485895

16660023

Properties and subcellular distribution of two partially purified ornithine transcarbamoylases in cell suspensions of sugarcane

1977

Glenn, E.; Maretzki, A.

Plant Physiol.

60

122-126

485896

16659361

Partial purification and properties of ornithine transcarbamoylase from Nostoc muscorum

1975

Boggess, S.F.; Naylor, A.W.

Plant Physiol.

56

640-644

485897

-

Control and properties of onithine transcarbamylase in germinated spores of Geotrichum candidum

1972

Barash, I.; Mor, H.

Plant Cell Physiol.

13

119-130

485898

4319

Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis

1976

Legrain, C.; Stalon, V.

Eur. J. Biochem.

63

289-301

485899

4613551

Interaction between arginase and L-ornithine carbamoyltransferase in Saccharomyces cerevisiae. Purification of S. cerevisiae enzymes and evidence that these enzymes as well as rat-liver arginase are trimers

1974

Penninckx, M.; Simon, J.P.; Wiame, J.M.

Eur. J. Biochem.

49

429-442

485900

16658053

Mode of action of the toxin from Pseudomonas phaseolicola. II. Mechanism of inhibition of bean ornithine carbamoyltransferase

1972

Tam, L.Q.; Patil, S.S.

Plant Physiol.

49

808-812

485901

16667466

Partial characterization of ornithine carbamoyltransferase in three microalgae

1990

Laliberte, G.; Hellebust, J.A.

Plant Physiol.

93

62-66

485902

-

Kinetic properties of carbamoyl-phosphate synthase (ammonia) and ornithine carbamoyltransferase in permeabilized mitochondria

1992

Cohen, N.S.; Cheung, C.W.; Sijuwade, E.; Raijman, L.

Biochem. J.

282

173-180

485903

11538003

Purification and characterization of ornithine transcarbamoylase from pea (Pisum sativum L.)

1991

Siocum, R.D.; Richardson, D.P.

Plant Physiol.

96

262-268

485904

3592910

Characterization of two ornithine carbamoyltransferases from Pseudomonas syringae pv. phaseolicola, the producer of phaseolotoxin

1987

Jahn, O.; Sauerstein, J.; Reuter, G.

Arch. Microbiol.

147

174-178

485905

16660512

Enzymes of Krebs-Henseleit cycle in Vitis vinifera L.

1978

Roubelakis, K.A.; Kliewer, W.M.

Plant Physiol.

62

337-339

485906

16664120

Properties of ornithine carbamoyltransferase from Pisum sativum L.

1985

De Ruiter, H.; Kollöffel, C.

Plant Physiol.

77

695-699

485907

-

Ornithine carbamoyltransferase of Streptomyces fradiae: purification and properties

1987

Szilagyi, I.; Vargha, G.; Szabo, G.

FEMS Microbiol. Lett.

48(1)

115-119

485908

5003693

Ornithine transcarbamylase: steady-state kinetic properties

1971

Kurtin, W.E.; Bishop, S.H.; Himoe, A.

Biochem. Biophys. Res. Commun.

45

551-556

485909

901452

N delta-(phosphonacetyl)-L-ornithine, a potent transition state analogue inhibitor of ornithine carbamoyltransferase

1977

Mori, M.; Aoyagi, K.; Tatibana, M.; Ishikawa, T.; Ishii, H.

Biochem. Biophys. Res. Commun.

76

900-904

485910

-

Separation and properties of two ornithine carbamoyltransferases from Pisum sativum seedlings

1974

Eid, S.; Waly, Y.; Abdelal, A.T.

Phytochemistry

13

99-102

485911

14923

Ornithine transcarbamylase from Salmonella typhimurium: purification, subunit composition, kinetic analysis, and immunological cross-reactivity

1977

Abdelal, A.T.H.; Kennedy, E.H.; Nainan, O.

J. Bacteriol.

129

1387-1396

485912

7356142

Purification of ornithine transcarbamylase from rat liver by affinity chromatography with immobilized transition-state analog

1980

Hoogenraad, N.J.; Sutherland, T.M.; Howlett, G.J.

Anal. Biochem.

101

97-102

485913

-

Purification and properties of ornithine carbamoyltransferase 1 from Alnus glutinosa root nodules

1983

Martin, F.; Hirel, B.; Gadal, P.

Z. Pflanzenphysiol.

111

413-422

485914

677887

Synthesis and properties of delta-N-(phosphonacetyl)-L-ornithine. A transition-state analog inhibitor of ornithine transcarbamylase

1978

Hoogenraad, N.J.

Arch. Biochem. Biophys.

188

137-144

485915

6767684

Stabilization and purification of ornithine transcarbamylase from Neisseria gonorrhoeae

1980

Powers, C.N.; Pierson, D.L.

J. Bacteriol.

141

544-549

485916

-

Characterization of ornithine carbamoyltransferase from cultured carrot cells of low embryogenic potential

1983

Baker, S.R.; Yon, R.J.

Phytochemistry

22

2171-2174

485917

4061826

High-performance hydrophobic interaction chromatography: purification of rat liver carbamoylphosphate synthetase I and ornithine transcarbamoylase

1985

Miller, N.T.; Feibush, B.; Corina, K.; Powers-Lee, S.; Karger, B.L.

Anal. Biochem.

148

510-517

485918

3159341

Ornithine transcarbamylase from Neurospora crassa: purification and properties

1985

Bates, M.; Weiss, R.L.; Clarke, S.

Arch. Biochem. Biophys.

239

172-183

485919

6418730

Chicken ornithine transcarbamylase: purification and some properties

1983

Tsuji, S.

J. Biochem.

94

1307-1315

485920

6393952

The inhibition of ornithine transcarbamoylase from Escherichia coli W by phaseolotoxin

1984

Templeton, M.D.; Sullivan, P.A.; Sheperd, M.G.

Biochem. J.

224

379-388

485921

6409880

Purification, characterization, and physiological function of Bacillus subtilis ornithine transcarbamylase

1983

Neway, J.O.; Switzer, R.L.

J. Bacteriol.

155

512-521

485922

2930186

Purification and properties of ornithine carbamoyl transferase from liver of Squalus acanthias

1989

Xiong, X.; Anderson, P.M.

Arch. Biochem. Biophys.

270

198-207

485923

489581

Ornithine transcarbamylase of rat liver. Kinetic, physical, and chemical properties

1979

Lusty, C.J.; Jilka, R.L.; Nietsch, E.H.

J. Biol. Chem.

254

10030-10036

485924

6771286

The essential sulfhydryl group of ornithine transcarbamylases. Reaction with anionic, aromatic disulfides and properties of its cyano derivative

1980

Marshall, M.; Cohen, P.P.

J. Biol. Chem.

255

7291-7295

485925

6370999

Purification and characterization of ornithine transcarbamoylase from Saccharomyces cerevisiae

1984

Eisenstein, E.; Osborn, J.C.; Chaiken, I.M.; Hensley, P.

J. Biol. Chem.

259

5139-5145

485926

893420

Human ornithine transcarbamylase. Purification and characterization of the enzyme from normal liver and the liver of a Reyes syndrome patient

1977

Pierson, D.L.; Cox, S.L.; Gilbert, B.E.

J. Biol. Chem.

252

6464-6469

485927

25896

Isolation and characterization of ornithine transcarbamylase from normal human liver

1978

Kalousek, F.; Francois, B.; Rosenberg, L.E.

J. Biol. Chem.

253

3939-3944

485928

8135541

Purification and properties of porcine liver ornithine transcarbamylase

1994

Koger, J.B.; Howell, R.G.; Kelly, M.; Jones, E.E.

Arch. Biochem. Biophys.

309

293-299

485929

8168544

Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Changes of allosteric properties resulting from modifications at the C-terminus

1994

Tricot, C.; Schmid, S.; Baur, H.; Villeret, V.; Dideberg, O.; Haas, D.; Stalon, V.

Eur. J. Biochem.

221

555-561

485930

7868583

Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization, sequence determination, and evolution

1995

Ruepp, A.; Mueller, H.N.; Lottspeich, F.; Soppa, J.

J. Bacteriol.

177

1129-1136

485932

9288930

Biochemical characterization of ornithine carbamoyltransferase from Pyrococcus furiosus

1997

Legrain, C.; Villeret, V.; Roovers, M.; Gigot, D.; Dideberg, O.; Pierard, A.; Glansdorff, N.

Eur. J. Biochem.

247

1046-1055

485933

-

Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonemia

1997

Morizono, H.; Tuchman, M.; Rajagopal, B.S.; McCann, M.T.; Listrom, C.D.; Yuan, X.; Venugopal, D.; Barany, G.; Allewell, N.M.

Biochem. J.

322

625-631

485934

9346304

Ornithine carbamoyltransferase from the extreme thermophile Thermus thermophilus. Analysis of the gene and characterization of the protein

1997

Sanchez, R.; Baetens, M.; Van De Casteele, M.; Roovers, M.; Legrain, C.; Glansdorff, N.

Eur. J. Biochem.

248

466-474

485935

9640663

Purification of ornithine carbamyltransferase from kidney bean (Phaseolus vulgaris) leaves and comparison of the properties of the enzyme from canavanine-containing and -deficient plants

1998

Lee, Y.; Jun, B.O.; Kim, S.G.; Kwon, Y.M.

Planta

205

375-379

485938

9492328

Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

1998

Sainz, G.; Tricot, C.; Foray, M.F.; Marion, D.; Dideberg, O.; Stalon, V.

Eur. J. Biochem.

251

528-533

485945

12108925

Purification and properties of ornithine carbamoyltransferase from loggerhead turtle liver

2002

Bellocco, E.; Di Salvo, C.; Lagana, G.; Leuzzi, U.; Tellone, E.; Kotyk, A.; Galtieri, A.

Physiol. Res.

51

151-158

485946

-

Ornithine carbamoyltransferase from Spinacia oleracea: purification and characterization

2002

Bellocco, E.; Di Salvo, C.; Lagana, G.; Galtieri, A.; Ficarra, S.; Kotyk, A.; Leuzzi, U.

Biol. Plant.

45

533-538

485957

7557411

Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3'-hydroxymethylcephem O-carbamoyltransferase for cephamycin biosynthesis

1995

Coque, J.J.R.; Perez-Llarena, F.J.; Enguita, F.J.; Fuente, J.L.; Martin, J.F.; Liras, P.

Gene

162

21-27

486063

16890

N-Acetylglutamate synthase of Escherichia coli: purification, characterization, and molecular properties

1977

Marvil, D.K.; Leisinger, T.

J. Biol. Chem.

252

3295-3303

639949

-

L-tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas sp.

1980

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

44

2013-2019

642353

6040410

Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II. Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway

1967

Farago, A.; Denes, G.

Biochim. Biophys. Acta

136

6-18

642356

240684

N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Catalytic and regulatory properties

1975

Haas, D.; Leisinger, T.

Eur. J. Biochem.

52

377-383

649104

-

Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase

1999

Lemke, C.; Yeung, M.; Howell, P.L.

Acta Crystallogr. Sect. D

55

2028-2030

650761

12618329

Resistance to the anti-proliferative activity of recombinant arginine deiminase in cell culture correlates with the endogenous enzyme, argininosuccinate synthetase

2003

Shen, L.J.; Lin, W.C.; Beloussow, K.; Shen, W.C.

Cancer Lett.

191

165-170

651026

-

A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization

2002

Geueke, B.; Hummel, W.

Enzyme Microb. Technol.

31

77-87

651195

12445581

L-citrulline recycling by argininosuccinate synthetase and lyase in rat gastric fundus

2002

Van Geldre, L.A.; Timmermans, J.P.; Lefebvre, R.A.

Eur. J. Pharmacol.

455

149-160

651600

15113205

Arginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis

2004

Lu, X.; Galkin, A.; Herzberg, O.; Dunaway-Mariano, D.

J. Am. Chem. Soc.

126

5374-5375

652188

11546769

Structural and functional characterization of the Zn(II) site in dimethylargininase-1 (DDAH-1) from bovine brain. Zn(II) release activates DDAH-1

2001

Knipp, M.; Charnock, J.M.; Garner, C.D.; Vasak, M.

J. Biol. Chem.

276

40449-40456

652231

11809762

Substrate induced conformational changes in argininosuccinate synthetase

2002

Lemke, C.T.; Howell, P.L.

J. Biol. Chem.

277

13074-13081

652242

11844799

Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action

2002

Goto, M.; Nakajima, Y.; Hirotsu, K.

J. Biol. Chem.

277

15890-15896

652404

12684518

Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms. Stereochemistry of the catalytic reaction

2003

Goto, M.; Omi, R.; Miyahara, I.; Sugahara, M.; Hirotsu, K.

J. Biol. Chem.

278

22964-22971

652976

11556547

Neuronal and glial coexpression of argininosuccinate synthetase and inducible nitric oxide synthase in Alzheimer disease

2001

Heneka, M.T.; Wiesinger, H.; Dumitrescu-Ozimek, L.; Riederer, P.; Feinstein, D.L.; Klockgether, T.

J. Neuropathol. Exp. Neurol.

60

906-916

653344

9879717

Inability of rat alveolar macrophages to recycle L-citrulline to L-arginine despite induction of argininosuccinate synthetase mRNA and protein, and inhibition of nitric oxide synthesis by exogenous L-citrulline

1998

Hammermann, R.; Bliesener, N.; Mossner, J.; Klasen, S.; Wiesinger, H.; Wessler, I.; Racke, K.

Naunyn Schmiedebergs Arch. Pharmacol.

358

601-607

661285

15820746

IL-1beta stimulates argininosuccinate synthetase gene expression through NF-kappaB in Caco-2 cells

2005

Brasse-Lagnel, C.; Lavoinne, A.; Fairand, A.; Vavasseur, K.; Husson, A.

Biochimie

87

403-409

662205

14970240

Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells

2004

Goodwin, B.L.; Solomonson, L.P.; Eichler, D.C.

J. Biol. Chem.

279

18353-18360

662254

15192091

Argininosuccinate synthetase is reversibly inactivated by S-nitrosylation in vitro and in vivo

2004

Hao, G.; Xie, L.; Gross, S.S.

J. Biol. Chem.

279

36192-36200

662377

15851478

Regulation of endothelial argininosuccinate synthase expression and NO production by an upstream open reading frame

2005

Pendleton, L.C.; Goodwin, B.L.; Solomonson, L.P.; Eichler, D.C.

J. Biol. Chem.

280

24252-24260

664807

3109911

Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli

1987

Baur, H.; Stalon, V.; Falmagne, P.; Luethi, E.; Haas, D.

Eur. J. Biochem.

166

111-117

665098

-

Tryptophanyl aminopeptidase

2004

Adachi, O.

Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)

2nd. ed.

1014-1015

666005

1906110

Molecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis

1991

Marcq, S.; Diaz-Ruano, A.; Charlier, P.; Dideberg, O.; Tricot, C.; Pierard, A.; Stalon, V.

J. Mol. Biol.

220

9-12

668755

-

Tryptophanyl aminopeptidase

2004

Adachi, O.

Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press

1

1014-1015

670913

16698551

Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: a basis for the design of specific inhibitors

2006

Frey, D.; Braun, O.; Briand, C.; Vašák, M.; Grütter, M.G.

Structure

14

901-911

675096

16420741

Liver argininosuccinate synthase binds to bacterial lipopolysaccharides and lipid A and inactivates their biological activities

2006

Satoh, M.; Iwahori, T.; Sugawara, N.; Yamazaki, M.

J. Endotoxin Res.

12

21-38

675890

16885415

Activity-dependent reversible inactivation of the general amino acid permease

2006

Risinger, A.L.; Cain, N.E.; Chen, E.J.; Kaiser, C.A.

Mol. Biol. Cell

17

4411-4419

676636

17142485

Enzymatic evidence for the key role of arginine in nitrogen translocation by arbuscular mycorrhizal fungi

2007

Cruz, C.; Egsgaard, H.; Trujillo, C.; Ambus, P.; Requena, N.; Martins-Loucao, M.A.; Jakobsen, I.

Plant Physiol.

144

782-792

686013

16847570

Brefeldin A decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae

2006

Alonso, M.; Burgos, H.I.; Pannunzio, V.; Hughes, A.M.; Mattoon, J.R.; Stella, C.A.

Cell. Mol. Biol. Lett.

11

256-263

690234

18323623

Structure of human argininosuccinate synthetase

2008

Karlberg, T.; Collins, R.; van den Berg, S.; Flores, A.; Hammarstroem, M.; Hoegbom, M.; Holmberg Schiavone, L.; Uppenberg, J.

Acta Crystallogr. Sect. D

64

279-286

690727

18375203

Troglitazone up-regulates vascular endothelial argininosuccinate synthase

2008

Goodwin, B.L.; Corbin, K.D.; Pendleton, L.C.; Levy, M.M.; Solomonson, L.P.; Eichler, D.C.

Biochem. Biophys. Res. Commun.

370

254-258

690765

18948083

Phosphorylation of argininosuccinate synthase by protein kinase A

2008

Corbin, K.D.; Pendleton, L.C.; Solomonson, L.P.; Eichler, D.C.

Biochem. Biophys. Res. Commun.

377

1042-1046

690768

18840401

Identification of a liver-specific cAMP response element in the human argininosuccinate synthetase gene

2008

Guei, T.R.; Liu, M.C.; Yang, C.P.; Su, T.S.

Biochem. Biophys. Res. Commun.

377

257-261

692607

18387919

Clearance of bacterial lipopolysaccharides and lipid A by the liver and the role of argininosuccinate synthase

2008

Satoh, M.; Ando, S.; Shinoda, T.; Yamazaki, M.

Innate Immun.

14

51-60

692659

18661517

Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase

2008

Bowles, T.L.; Kim, R.; Galante, J.; Parsons, C.M.; Virudachalam, S.; Kung, H.J.; Bold, R.J.

Int. J. Cancer

123

1950-1955

693030

18263583

An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability

2008

Zhao, Y.; Zhang, J.; Li, H.; Li, Y.; Ren, J.; Luo, M.; Zheng, X.

J. Biol. Chem.

283

11004-11013

700356

19060912

Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor

2009

Van Zeebroeck, G.; Bonini, B.M.; Versele, M.; Thevelein, J.M.

Nat. Chem. Biol.

5

45-52

701115

19507245

X-ray structure and kinetic properties of ornithine transcarbamoylase from the human parasite Giardia lamblia

2009

Galkin, A.; Kulakova, L.; Wu, R.; Gong, M.; Dunaway-Mariano, D.; Herzberg, O.

Proteins Struct. Funct. Bioinform.

76

1049-1053

711211

19663506

Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide

2009

Wang, Y.; Monzingo, A.F.; Hu, S.; Schaller, T.H.; Robertus, J.D.; Fast, W.

Biochemistry

48

8624-8635

711874

21048866

A simple enzymatic method for production of a wide variety of D-amino acids using L-amino acid oxidase from Rhodococcus sp. AIU Z-35-1

2010

Isobe, K.; Tamauchi, H.; Fuhshuku, K.; Nagasawa, S.; Asano, Y.

Enzyme Res.

2010

567210

720104

21515096

N-Carbamoyl-beta-alanine amidohydrolase from Agrobacterium tumefaciens C58: a promiscuous enzyme for the production of amino acids

2011

Martinez-Gomez, A.I.; Andujar-Sanchez, M.; Clemente-Jimenez, J.M.; Neira, J.L.; Rodriguez-Vico, F.; Martinez-Rodriguez, S.; Las Heras-Vazquez, F.J.

J. Chromatogr. B

879

3277-3282

720414

21471002

Transport activity-dependent intracellular sorting of the yeast general amino acid permease

2011

Cain, N.E.; Kaiser, C.A.

Mol. Biol. Cell

22

1919-1929

725629

-

Pathways of arginine biosynthesis in extreme thermophilic archaeo- and eubacteria

1990

Van de Casteele, M.; Demarez, M.; Legrain, C.; Glansdorff, N.; Pierard, A.

J. Gen. Microbiol.

136

1177-1183

726863

22001918

Site-specific incorporation of arginine analogs into proteins using arginyl-tRNA synthetase

2011

Akahoshi, A.; Suzue, Y.; Kitamatsu, M.; Sisido, M.; Ohtsuki, T.

Biochem. Biophys. Res. Commun.

414

625-630

728544

23094117

Leishmania donovani argininosuccinate synthase is an active enzyme associated with parasite pathogenesis

2012

Lakhal-Naouar, I.; Jardim, A.; Strasser, R.; Luo, S.; Kozakai, Y.; Nakhasi, H.L.; Duncan, R.C.

PLoS Negl. Trop. Dis.

6

e1849

735216

23867361

Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49

2013

Hering, S.; Sieg, A.; Kreikemeyer, B.; Fiedler, T.

Protein Expr. Purif.

91

61-68

736594

25492493

Improvement of L-citrulline production in Corynebacterium glutamicum by ornithine acetyltransferase

2015

Hao, N.; Mu, J.; Hu, N.; Xu, S.; Yan, M.; Li, Y.; Guo, K.; Xu, L.

J. Ind. Microbiol. Biotechnol.

42

307-313

749045

26939071

Genetic manipulation of Leishmania donovani to explore the involvement of argininosuccinate synthase in oxidative stress management

2016

Sardar, A.; Jardim, A.; Ghosh, A.; Mandal, A.; Das, S.; Saini, S.; Abhishek, K.; Singh, R.; Verma, S.; Kumar, A.; Das, P.

PLoS Negl. Trop. Dis.

10

e0004308

753986

-

The expression, purification and activity analysis of Francisella tularensis citrulline ureidase in Escherichia coli

2015

Zhu, T.; Fang, S.; Wang, W.; Wang, K.; Cui, Z.; Wang, C.

J. Appl. Biomed.

13

189-194