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Literature summary for 2.7.3.3 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)

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

Protein Variants

Protein Variants Comment Organism
G54A the mutant shows considerably increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis
G54I the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
G54L the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
G54S the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis
G54V the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
L64A the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
L64G the mutant displays undetectable enzymatic activity Sabellastarte spectabilis
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
L64V the mutant shows a 1.7fold decrease in affinity for L-arginine, but unchanged affinity for D-arginine Sabellastarte spectabilis
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
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
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
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
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
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
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
Y89Q the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme Sabellastarte spectabilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.389
-
L-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
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
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
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
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
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
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
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
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
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
2.05
-
L-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
2.72
-
L-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
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
3.14
-
D-Arg isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
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
3.69
-
L-Arg wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
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
4.4
-
D-Arg isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
5.07
-
L-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
6.45
-
L-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
6.45
-
D-Arg isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
9
-
D-Arg wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
9.34
-
D-Arg isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis
9.55
-
D-Arg isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C Sabellastarte spectabilis

Organism

Organism UniProt Comment Textmining
Sabellastarte spectabilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
ATP + L-Arg isoforms AK1 and AK2 are primarily active towards L-arginine Sabellastarte spectabilis ADP + Nomega-phospho-L-Arg
-
?

Synonyms

Synonyms Comment Organism
AK1 isoform Sabellastarte spectabilis
AK2 isoform Sabellastarte spectabilis

Turnover Number [1/s]

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

kcat/KM [mM/s]

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