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Literature summary extracted from

  • Nagata, R.; Fujihashi, M.; Sato, T.; Atomi, H.; Miki, K.
    Crystal structure and product analysis of an archaeal myo-inositol kinase reveal substrate recognition mode and 3-OH phosphorylation (2015), Biochemistry, 54, 3494-3503.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.64 complexed with an ATP analogue and myo-inositol, hanging drop vapor diffusion method, using Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.64 ATP + myo-inositol Thermococcus kodakarensis
-
 ADP + 1D-myo-inositol 3-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.64 Thermococcus kodakarensis Q5JDA3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.64 ATP + myo-inositol
-
 Thermococcus kodakarensis ADP + 1D-myo-inositol 3-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.64 MI3K
-
 Thermococcus kodakarensis
2.7.1.64 myo-inositol 3-kinase
-
 Thermococcus kodakarensis
2.7.1.64 myo-inositol kinase
-
 Thermococcus kodakarensis
2.7.1.64 TK2285 protein
-
 Thermococcus kodakarensis