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Literature summary for 2.7.1.1 extracted from

  • Nakamura, T.; Kashima, Y.; Mine, S.; Oku, T.; Uegaki, K.
    Characterization and crystal structure of the thermophilic ROK hexokinase from Thermus thermophilus (2012), J. Biosci. Bioeng., 114, 150-154 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the enzyme is determined at a resolution of 2.02 A Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SLJ4
-
-
Thermus thermophilus DSM 579 Q5SLJ4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glucose
-
Thermus thermophilus ADP + D-glucose 6-phosphate
-
?
ATP + D-glucose
-
Thermus thermophilus DSM 579 ADP + D-glucose 6-phosphate
-
?
ATP + D-mannose
-
Thermus thermophilus ADP + D-mannose 6-phosphate
-
?
ATP + D-mannose
-
Thermus thermophilus DSM 579 ADP + D-mannose 6-phosphate
-
?
additional information the enzyme shows little catalytic capacity for galactose and fructose Thermus thermophilus ?
-
?
additional information the enzyme shows little catalytic capacity for galactose and fructose Thermus thermophilus DSM 579 ?
-
?

Subunits

Subunits Comment Organism
homotetramer consists of a dimer of dimers Thermus thermophilus

Synonyms

Synonyms Comment Organism
ROK hexokinase
-
Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
circular dichroism measurements indicates that the enzyme is structurally stable at 90°C Thermus thermophilus