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Literature summary extracted from

  • Yeh, J.I.; Kettering, R.; Saxl, R.; Bourand, A.; Darbon, E.; Joly, N.; Briozzo, P.; Deutscher, J.
    Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation (2009), Biochemistry, 48, 346-356.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.30 His-tag, expressed in Escherichia coli Enterococcus casseliflavus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.30
-
 Enterococcus casseliflavus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.30 H232A residue located in the activation loop Enterococcus casseliflavus
2.7.1.30 H232E residue located in the activation loop Enterococcus casseliflavus
2.7.1.30 H232R residue located in the activation loop, mutant protein has enhanced activity Enterococcus casseliflavus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.30 Enterococcus casseliflavus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.30 additional information activity is enhanced phosphorylation of His232 Enterococcus casseliflavus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.30
-
 Enterococcus casseliflavus

Subunits

EC Number Subunits Comment Organism
2.7.1.30 homodimer crystal structure Enterococcus casseliflavus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.30 glycerol kinase
-
 Enterococcus casseliflavus