Literature summary for 2.7.1.11 extracted from

Webb, B.A.; Forouhar, F.; Szu, F.E.; Seetharaman, J.; Tong, L.; Barber, D.L.
Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations (2015), Nature, 523, 111-114.

Application

Application	Comment	Organism
medicine	somatic PFK1 mutations identified in human cancers have distinct effects on allosteric regulation of enzymic activity and lactate production	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of the mammalian 6-phosphofructokinase PFK1 tetramer, for the human platelet isoform, in complex with MgATPMg2- and ADP at 3.1 and 3.4 A resolution, respectively. The structures reveal substantial conformational changes in the enzyme upon nucleotide hydrolysis as well as a unique tetramer interface. Mutations of residues in this interface can affect tetramer formation, enzyme catalysis and regulation. Somatic PFK1 mutations identified in human cancers have distinct effects on allosteric regulation of enzymic activity and lactate production	Homo sapiens

Crystallization (Comment)

Organism

structures of the mammalian 6-phosphofructokinase PFK1 tetramer, for the human platelet isoform, in complex with MgATPMg2- and ADP at 3.1 and 3.4 A resolution, respectively. The structures reveal substantial conformational changes in the enzyme upon nucleotide hydrolysis as well as a unique tetramer interface. Mutations of residues in this interface can affect tetramer formation, enzyme catalysis and regulation. Somatic PFK1 mutations identified in human cancers have distinct effects on allosteric regulation of enzymic activity and lactate production

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D564N	somatic mutation identified in human cancers. Mutant has decreased maximum velocity and affinity for fructose 6-phosphate	Homo sapiens
E657A	mutant has reduced affinity of about 4.5 mM for frucotse 6-phosphate, compared with about 0.8 mM in wild type, and an 2fold decrease in maximum activity	Homo sapiens
N426S	somatic mutation identified in human cancers. Mutation partially relieves ATP inhibition	Homo sapiens
R48C	somatic mutation identified in human cancers. Residue Arg48 interacts with a bound phosphate ion in the structure, and the mutant shows reduced citrate inhibition	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q01813	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood platelet	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
PFK1	-	Homo sapiens