{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fernandes PM"],"funding":["Medical Research Council","Wellcome Trust"],"pagination":["4425-4441"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7702303"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["477(22)"],"pubmed_abstract":["6-Phosphofructokinase-1-kinase (PFK) tetramers catalyse the phosphorylation of fructose 6-phosphate (F6P) to fructose 1,6-bisphosphate (F16BP). Vertebrates have three PFK isoforms (PFK-M, PFK-L, and PFK-P). This study is the first to compare the kinetics, structures, and transcript levels of recombinant human PFK isoforms. Under the conditions tested PFK-M has the highest affinities for F6P and ATP (K0.5ATP 152 µM; K0.5F6P 147 µM), PFK-P the lowest affinities (K0.5ATP 276 µM; K0.5F6P 1333 µM), and PFK-L demonstrates a mixed picture of high ATP affinity and low F6P affinity (K0.5ATP 160 µM; K0.5F6P 1360 µM). PFK-M is more resistant to ATP inhibition compared with PFK-L and PFK-P (respectively, 23%, 31%, 50% decreases in specificity constants). GTP is an alternate phospho donor. Interface 2,"],"journal":["The Biochemical journal"],"pubmed_title":["Biochemical and transcript level differences between the three human phosphofructokinases show optimisation of each isoform for specific metabolic niches."],"pmcid":["PMC7702303"],"funding_grant_id":["MC_PC_16043","106359"],"pubmed_authors":["Fernandes PM","Walkinshaw MD","Michels PAM","McNae I","Kinkead J"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical and transcript level differences between the three human phosphofructokinases show optimisation of each isoform for specific metabolic niches.","description":"6-Phosphofructokinase-1-kinase (PFK) tetramers catalyse the phosphorylation of fructose 6-phosphate (F6P) to fructose 1,6-bisphosphate (F16BP). Vertebrates have three PFK isoforms (PFK-M, PFK-L, and PFK-P). This study is the first to compare the kinetics, structures, and transcript levels of recombinant human PFK isoforms. Under the conditions tested PFK-M has the highest affinities for F6P and ATP (K0.5ATP 152 µM; K0.5F6P 147 µM), PFK-P the lowest affinities (K0.5ATP 276 µM; K0.5F6P 1333 µM), and PFK-L demonstrates a mixed picture of high ATP affinity and low F6P affinity (K0.5ATP 160 µM; K0.5F6P 1360 µM). PFK-M is more resistant to ATP inhibition compared with PFK-L and PFK-P (respectively, 23%, 31%, 50% decreases in specificity constants). GTP is an alternate phospho donor. Interface 2,","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2026-05-08T16:24:23.07Z","creation":"2021-02-20T09:40:33Z"},"accession":"S-EPMC7702303","cross_references":{"pubmed":["33141153"],"doi":["10.1042/BCJ20200656"]}}