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Literature summary extracted from

  • Uda, K.; Matumoto, A.; Suzuki, T.
    Identification of the key amino acid residues in Sabellastarte arginine kinase for distinguishing chiral guanidino substrates (d- and l-arginine) (2010), J. Mol. Catal. B, 64, 75-80.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.3 isoform AK2 fused to maltose-binding protein is expressed in Escherichia coli TB1 cells Sabellastarte spectabilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.3.3 G54A the mutant shows considerably increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis
2.7.3.3 G54I the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
2.7.3.3 G54L the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
2.7.3.3 G54S the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis
2.7.3.3 G54V the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
2.7.3.3 L64A the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
2.7.3.3 L64G the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
2.7.3.3 L64I in the mutant, the affinity for L-arginine is greatly increased (9.5fold that of the wild type), whereas its affinity for D-arginine is increased 2.9fold Sabellastarte spectabilis
2.7.3.3 L64V the mutant shows a 1.7fold decrease in affinity for L-arginine, but unchanged affinity for D-arginine Sabellastarte spectabilis
2.7.3.3 N320A the mutant shows considerably reduced enzymatic activity (17.1% for L-arginine and 5.19% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320D the mutant shows considerably reduced enzymatic activity (32.4% for L-arginine and 48.4% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320E the mutant shows considerably reduced enzymatic activity (52.3% for L-arginine and 10.1% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320H the mutant shows considerably reduced enzymatic activity (29.5% for L-arginine and 10.2% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320K the mutant shows considerably reduced enzymatic activity (0.612% for L-arginine and 0.489% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320Q the mutant shows considerably reduced enzymatic activity (8.97% for L-arginine and 2,6% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 N320R the mutant shows considerably reduced enzymatic activity (4.11% for L-arginine and 1.46% for D-arginine compared to the wild type enzyme) Sabellastarte spectabilis
2.7.3.3 Y89Q the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.3 0.389
-
 L-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.4
-
 ATP isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.661
-
 ATP isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.774
-
 ATP isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.837
-
 ATP isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.926
-
 ATP isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 0.93
-
 ATP isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 1.12
-
 ATP isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 1.13
-
 ATP wild type enzyme isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 1.59
-
 ATP isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 2.05
-
 L-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 2.72
-
 L-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 2.99
-
 ATP wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 3.14
-
 D-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 3.49
-
 ATP isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 3.69
-
 L-Arg wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 3.72
-
 ATP isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 4.4
-
 D-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 5.07
-
 L-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 6.45
-
 L-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 6.45
-
 D-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9
-
 D-Arg wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.34
-
 D-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.55
-
 D-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.3 Sabellastarte spectabilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.3 ATP + D-Arg isoform AK1 shows 7.6% activity with D-arginine compared to L-arginine, isoform AK2 shows 35% activity with D-arginine compared to L-arginine Sabellastarte spectabilis ADP + Nomega-phospho-D-Arg
-
 ?
2.7.3.3 ATP + L-Arg isoforms AK1 and AK2 are primarily active towards L-arginine Sabellastarte spectabilis ADP + Nomega-phospho-L-Arg
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.3.3 AK1 isoform Sabellastarte spectabilis
2.7.3.3 AK2 isoform Sabellastarte spectabilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.3.3 33.4
-
 ATP isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 36.6
-
 ATP wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 39.5
-
 ATP wild type isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 40.8
-
 D-Arg wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 41
-
 ATP isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 41.9
-
 ATP isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 43.2
-
 ATP isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 43.3
-
 ATP isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 46
-
 L-Arg wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 50.1
-
 ATP isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 60.7
-
 ATP isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 61.5
-
 D-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 61.8
-
 ATP isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 62.3
-
 L-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 65.8
-
 ATP isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 68.3
-
 ATP isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 75.4
-
 L-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 77.8
-
 L-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 81.2
-
 L-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 86.7
-
 D-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 90.7
-
 D-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 90.7
-
 D-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 121
-
 L-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 121
-
 D-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.3.3 4.52
-
 D-Arg wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.29
-
 D-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.52
-
 D-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.54
-
 D-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 9.65
-
 L-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 12.5
-
 L-Arg wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 15.4
-
 L-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 27.5
-
 D-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 29
-
 D-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 39.5
-
 L-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 44.7
-
 L-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.7.3.3 195
-
 L-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis