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Literature summary for 2.7.1.130 extracted from

  • Emptage, R.P.; Daughtry, K.D.; Pemble, C.W.; Raetz, C.R.
    Crystal structure of LpxK, the 4-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface (2012), Proc. Natl. Acad. Sci. USA, 109, 12956-12961.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base Aquifex aeolicus

Protein Variants

Protein Variants Comment Organism
D138A point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity Aquifex aeolicus
D139A point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity Aquifex aeolicus
G47A about 43% of wild-type activity Aquifex aeolicus
G48A about 1.8% of wild-type activity Aquifex aeolicus
G50A about 0.1% of wild-type activity Aquifex aeolicus
K51A about 0.1% of wild-type activity Aquifex aeolicus
S53A about 9.9% of wild-type activity Aquifex aeolicus
T52A about 0.1% of wild-type activity Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O67572
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Synonyms

Synonyms Comment Organism
LpxK
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Aquifex aeolicus