Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.30 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Enterococcus casseliflavus

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Enterococcus casseliflavus
-
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
-
Enterococcus casseliflavus

Subunits

Subunits Comment Organism
homodimer crystal structure Enterococcus casseliflavus

Synonyms

Synonyms Comment Organism
glycerol kinase
-
Enterococcus casseliflavus