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Literature summary for 2.7.3.3 extracted from

  • Guo, Q.; Zhao, F.; Guo, S.Y.; Wang, X.
    The tryptophane residues of dimeric arginine kinase: roles of Trp-208 and Trp-218 in active site and conformation stability (2004), Biochimie, 86, 379-386.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
W208A mutant enzyme shows 70.3% of the wild-type enzyme in the forward reaction. Mutation makes the enzyme susceptible to heat and denaturants, sich as guanidine HCl Apostichopus japonicus
W218A mutation causes almost complete loss of activity and decreases the melting temperature in differential scanning calometry profiles and decreases stability against guanidine hydrochloride denaturation Apostichopus japonicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
ATP pH 8.1, mutant enzyme W208A Apostichopus japonicus
0.48
-
ATP pH 8.1, wild-type enzyme Apostichopus japonicus
0.66
-
L-arginine pH 8.1, wild-type enzyme Apostichopus japonicus
0.7
-
L-arginine pH 8.1, mutant enzyme W208A Apostichopus japonicus

Organism

Organism UniProt Comment Textmining
Apostichopus japonicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Apostichopus japonicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine
-
Apostichopus japonicus ADP + Nomega-phosphono-L-arginine
-
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