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1 has been predicted to have only independent phosphoglycerate mutase.
2 with similarities to the catalytic motif of phosphoglycerate mutase.
3 and His141, are not parallel as in the yeast phosphoglycerate mutase.
5 recently reported that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1) regulates anabolic bio
7 rs, covalently labeled the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), resulting in enzyme i
9 yaluronan synthase 2) and Bevacizumab/PGAM1 (Phosphoglycerate mutase 1) are interactions found in thi
10 Here, we reveal that the glycolytic enzyme phosphoglycerate mutase-1 (PGAM1) is negatively regulate
11 lism by overexpressing the glycolytic enzyme phosphoglycerate mutase-1 severely impaired the ability
12 nd filamin-C), glycolytic enzymes (aldolase, phosphoglycerate mutase 2, beta enolase and glycogen pho
13 0 MPa) provoked a significant degradation of phosphoglycerate mutase 2, glycogen phosphorylase muscle
14 to extend Drosophila lifespan, and identify Phosphoglycerate Mutase 5 (PGAM5) as a mediator of this
17 veals that it has homology to members of the phosphoglycerate mutase/acid phosphatase (PGM/AcP) famil
18 lysis and recombinant enzymes showed typical phosphoglycerate mutase activities in both the glycolyti
21 rtially associated with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily re
22 ru-2,6-P2ase is similar to that of the yeast phosphoglycerate mutase and the rat prostatic acid phosp
24 otide ubiquinone oxidoreductase chain 2, and phosphoglycerate mutase B], ion regulation (members of s
25 s similar to the group of cofactor-dependent phosphoglycerate mutase/bisphosphoglycerate mutase enzym
29 cture of Escherichia coli cofactor-dependent phosphoglycerate mutase (dPGM), complexed with the poten
31 three steps of the lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase).
33 ere, we present evidence that members of the phosphoglycerate mutase family 5 (PGAM5) proteins are in
34 her found that the mitochondrial phosphatase phosphoglycerate mutase family member 5 (PGAM5), a putat
35 ice deficient for the mitochondrial protein, phosphoglycerate mutase family member 5 (PGAM5), display
36 alytic domains found in other members of the phosphoglycerate mutase family, including a conserved hi
37 is report we have identified a member of the phosphoglycerate mutase family, PGAM5, as a novel substr
38 present at the active site of the monomeric phosphoglycerate mutase from the fission yeast Schizosac
39 cloned and produced recombinant, independent phosphoglycerate mutases from C. elegans and the human-p
41 lis, Treponema pallidum, the gene encoding 3-phosphoglycerate mutase, gpm, is part of a six-gene oper
43 new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2
44 a typical nucleotide binding fold, although phosphoglycerate mutase has no physiological requirement
45 des, unlike vertebrates, utilize independent phosphoglycerate mutase in glycolytic and gluconeogenic
46 pH results in greatly decreased activity of phosphoglycerate mutase in the forespore, which in turn
47 lycolysis (glucose-6-phosphate isomerase and phosphoglycerate mutase), in trehalose-6-P metabolism (t
48 ween the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearotherm
51 of Leishmania mexicana cofactor-independent phosphoglycerate mutase (Lm iPGAM) crystallised with the
52 double labelled (15N,13C) monomeric, 23.7 kD phosphoglycerate mutase (PGAM) from Schizosaccharomyces
53 Here we report the interaction of Pak with phosphoglycerate mutase (PGAM)-B, an enzyme of the glyco
54 the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells
55 atase activity located within its C-terminal phosphoglycerate mutase (PGM) homology domain and key fo
56 the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first
62 mer-specific autophosphorylation of NME1 and phosphoglycerate mutase were used with immunoblotting an
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