Fructokinase
From Proteopedia
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'''Fructokinase''' (FRK) catalyzes the phosphorylation of fructose to fructose-1-phosphate using ATP as phosphate source in plants, bacteria and animals. In plants and bacteria FRK regulates starch synthesis. In animals it produces oxalate and its precursors<ref>PMID:3009653</ref>. | '''Fructokinase''' (FRK) catalyzes the phosphorylation of fructose to fructose-1-phosphate using ATP as phosphate source in plants, bacteria and animals. In plants and bacteria FRK regulates starch synthesis. In animals it produces oxalate and its precursors<ref>PMID:3009653</ref>. | ||
| - | + | *<scene name='48/484862/Cv/5'>Fructokinase with ADP and Fructose bound in the active site</scene> ([[3lm9]]). | |
== Relevance == | == Relevance == | ||
Revision as of 13:34, 8 June 2016
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3D structures of fructokinase
Updated on 08-June-2016
2qhp – FRK – Bacterioides thetaiotamicron
3ljs – XfFRK – Xylella fastidiosa
3hj6 – FRK – Halothermothrix orenii
3lki – XfFRK + ATP
3lm9 - BsFRK + ATP + fructose – Bacillus subtilis
3ohr - BsFRK + ADP
2v78, 2var – FRK – Sulfolobus solfataricus
3c8u – FRK – Silicibacter
References
- ↑ James HM, Williams SG, Bais R, Rofe AM, Edwards JB, Conyers RA. The metabolic production of oxalate from xylitol: activities of transketolase, transaldolase, fructokinase and aldolase in liver, kidney, brain, heart and muscle in the rat, mouse, guinea pig, rabbit and human. Int J Vitam Nutr Res Suppl. 1985;28:29-46. PMID:3009653
- ↑ Phillips MI, Davies DR. The mechanism of guanosine triphosphate depletion in the liver after a fructose load. The role of fructokinase. Biochem J. 1985 Jun 15;228(3):667-71. PMID:2992452
