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Literature summary for 2.7.3.3 extracted from

  • Strong, S.J.; Ellington, W.R.
    Expression of horseshoe crab arginine kinase in Escherichia coli and site-directed mutations of the reactive cysteine peptide (1996), Comp. Biochem. Physiol. B, 113, 809-816.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Limulus polyphemus

Protein Variants

Protein Variants Comment Organism
additional information double mutant Val268insertion/Phe270deletion: enzyme with significaltly decreased specific activity compared with both the native and the recombinant wild-type enzyme, no detectable change in guanidine substrate specificity Limulus polyphemus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Limulus polyphemus

Organism

Organism UniProt Comment Textmining
Limulus polyphemus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Limulus polyphemus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.245
-
homogenous muscle enzyme Limulus polyphemus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Limulus polyphemus ADP + Nomega-phospho-L-Arg
-
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