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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.3 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

EC Number Protein Variants Comment Organism
2.7.3.3 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
2.7.3.3 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

EC Number Organism UniProt Comment Textmining
2.7.3.3 Anthopleura japonica O15992
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.3.3 129
-
 L-Arg recombinant wild-type enzyme with MBP tag Anthopleura japonica
2.7.3.3 129
-
 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