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Literature summary for 3.1.3.46 extracted from

  • Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
    Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding (2017), Proteins, 85, 117-124 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens
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Bos taurus

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.8 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ADP, ADP mimicks the catalytic binding mode of ATP Bos taurus
to 2.0 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ATP analogue AMPPNP, the presence of a gamma-phosphate makes adoption of the catalytic ATP binding mode impossible for AMPPNP, forcing the analogue to bind atypically with concomitant conformational changes to the ATP binding-pocket Homo sapiens

Organism

Organism UniProt Comment Textmining
Bos taurus P26285 isoform PFKFB2, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
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Homo sapiens O60825 isoform PFKFB2, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
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Synonyms

Synonyms Comment Organism
PFKFB2
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Homo sapiens
PFKFB2
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Bos taurus