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Literature summary for 2.7.3.3 extracted from

  • Tada, H.; Nishimura, Y.; Suzuki, T.
    Cooperativity in the two-domain arginine kinase from the sea anemone Anthopleura japonicus (2008), Int. J. Biol. Macromol., 42, 46-51.
    View publication on PubMed
Search for more literature for 2.7.3.3

Cloned(Commentary)

Cloned (Comment) Organism
cDNAs of the two-domain arginine kinase and its separated domains 1 and 2 from Anthopleura japonicus, are cloned into the plasmid pMAL, and recombinant enzymes are expressed in Escherichia coli as MBP fusion proteins Anthopleura japonica

Protein Variants

Protein Variants Comment Organism
D62E introduction of Glu at position 62 in isolated domain 2. The catalytic efficiency of D2/D62E is similar to that of the two-domain wild-type enzyme. This replacement does not alter synergistic substrate binding relative to wild-type domain 2 Anthopleura japonica
D62G introduction of Gly at position 62 in isolated domain 2. The catalytic efficiency of the D2/D62G mutant is decreased to 13% that of wild-type domain 2 Anthopleura japonica

Organism

Organism UniProt Comment Textmining
Anthopleura japonica O15992
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
 Anthopleura japonica ADP + omega-N-phospho-L-Arg
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
129
-
 L-Arg recombinant wild-type enzyme with MBP tag Anthopleura japonica
129
-
 ATP recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains Anthopleura japonica