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Literature summary for 2.7.3.1 extracted from

  • Lim, K.; Pullalarevu, S.; Surabian, K.T.; Howard, A.; Suzuki, T.; Moult, J.; Herzberg, O.
    Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member (2010), Biochemistry, 49, 2031-2041.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Namalycastis sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structures of recombinant glycocyamine kinase alphabeta and glycocyamine kinase betabeta from Namalycastis sp. are determined at 2.6 A and 2.4 A resolution, respectively. In addition, the structure of the glycocyamine kinase betabeta is determined at 2.3 A resolution in complex with a transition state analog, Mg2+ ADP-NO3- glycocyamine. In both heterodimeric and homodimeric glycocyamine kinase forms, the conformations of the two N-termini are asymmetric and the asymmetry is different than that reported previously for the homodimeric creatinine kinases from several organisms Namalycastis sp.

Organism

Organism UniProt Comment Textmining
Namalycastis sp. Q6AW42
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Namalycastis sp.

Subunits

Subunits Comment Organism
heterodimer heterodimer with two homologous polypeptide chains, alpha and beta, derived from a common pre mRNA by mutually exclusive N-terminal alternative exons Namalycastis sp.

Synonyms

Synonyms Comment Organism
glycocyamine kinase
-
Namalycastis sp.