ライフサイエンスコーパス: phosphoglycerate mutase

1 ons with the glycolytic enzymes Aldolase and Phosphoglycerate mutase.

2 has been predicted to have only independent phosphoglycerate mutase.

3 with similarities to the catalytic motif of phosphoglycerate mutase.

4 and His141, are not parallel as in the yeast phosphoglycerate mutase.

5 Phosphoglycerate mutase 1 (PGAM1) functions in glycolysi

6 recently reported that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1) regulates anabolic bio

7 We found that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated

8 rs, covalently labeled the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), resulting in enzyme i

9 nts an additional acute mechanism underlying phosphoglycerate mutase 1 upregulation.

10 aracterized (pyruvate kinase muscle isozyme, phosphoglycerate mutase 1) and two uncharacterized (glut

11 yaluronan synthase 2) and Bevacizumab/PGAM1 (Phosphoglycerate mutase 1) are interactions found in thi

12 tion factor eEF1A1, and the metabolic enzyme phosphoglycerate mutase 1, or PGAM1, for which methylati

13 Here, we reveal that the glycolytic enzyme phosphoglycerate mutase-1 (PGAM1) is negatively regulate

14 lism by overexpressing the glycolytic enzyme phosphoglycerate mutase-1 severely impaired the ability

15 The proteins phosphoglycerate mutase 2 (P. squamosissimus), hemoglobi

16 nd filamin-C), glycolytic enzymes (aldolase, phosphoglycerate mutase 2, beta enolase and glycogen pho

17 0 MPa) provoked a significant degradation of phosphoglycerate mutase 2, glycogen phosphorylase muscle

18 to extend Drosophila lifespan, and identify Phosphoglycerate Mutase 5 (PGAM5) as a mediator of this

19 Phosphoglycerate mutase 5 (PGAM5) is an atypical mitocho

20 activation of the mitochondrial phosphatase phosphoglycerate mutase 5 (PGAM5).

21 augmented processing of a downstream target, phosphoglycerate mutase 5, at baseline and in response t

22 veals that it has homology to members of the phosphoglycerate mutase/acid phosphatase (PGM/AcP) famil

23 lysis and recombinant enzymes showed typical phosphoglycerate mutase activities in both the glycolyti

24 Five of these (phosphoglycerate mutase, alcohol dehydrogenase, thioredo

25 f enzymes such as triosephosphate isomerase, phosphoglycerate mutase, alpha-enolase, beta-enolase, fr

26 We provide evidence that phosphoglycerate mutase and enolase form a substrate-cha

27 New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were ide

28 rtially associated with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily re

29 ru-2,6-P2ase is similar to that of the yeast phosphoglycerate mutase and the rat prostatic acid phosp

30 etal transport system, the glycolytic enzyme phosphoglycerate mutase, and TroR.

31 otide ubiquinone oxidoreductase chain 2, and phosphoglycerate mutase B], ion regulation (members of s

32 s similar to the group of cofactor-dependent phosphoglycerate mutase/bisphosphoglycerate mutase enzym

33 We have identified a phosphoglycerate mutase brain isoform (PGAM 1, PGAM B) c

34 Phosphoglycerate mutases catalyze the interconversion of

35 The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology

36 cture of Escherichia coli cofactor-dependent phosphoglycerate mutase (dPGM), complexed with the poten

37 ilarity to 2, 3-diphosphoglycerate-dependent phosphoglycerate mutases (dPGM).

38 three steps of the lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase).

39 Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as a

40 ere, we present evidence that members of the phosphoglycerate mutase family 5 (PGAM5) proteins are in

41 ed mixed lineage kinase-like protein (MLKL), phosphoglycerate mutase family 5 (PGAM5), dynamin-relate

42 e demonstrate that the mitochondrial protein phosphoglycerate mutase family member 5 (PGAM5) is impor

43 her found that the mitochondrial phosphatase phosphoglycerate mutase family member 5 (PGAM5), a putat

44 ice deficient for the mitochondrial protein, phosphoglycerate mutase family member 5 (PGAM5), display

45 alytic domains found in other members of the phosphoglycerate mutase family, including a conserved hi

46 is report we have identified a member of the phosphoglycerate mutase family, PGAM5, as a novel substr

47 present at the active site of the monomeric phosphoglycerate mutase from the fission yeast Schizosac

48 cloned and produced recombinant, independent phosphoglycerate mutases from C. elegans and the human-p

49 (TroR), and the essential glycolytic enzyme phosphoglycerate mutase (Gpm).

50 lis, Treponema pallidum, the gene encoding 3-phosphoglycerate mutase, gpm, is part of a six-gene oper

51 rystal structure of Saccharomyces cerevisiae phosphoglycerate mutase has been determined.

52 new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2

53 a typical nucleotide binding fold, although phosphoglycerate mutase has no physiological requirement

54 to investigate the influence of crowding on phosphoglycerate mutase in Escherichia coli, which exhib

55 des, unlike vertebrates, utilize independent phosphoglycerate mutase in glycolytic and gluconeogenic

56 pH results in greatly decreased activity of phosphoglycerate mutase in the forespore, which in turn

57 lycolysis (glucose-6-phosphate isomerase and phosphoglycerate mutase), in trehalose-6-P metabolism (t

58 S to a luminescence assay for the isoform of phosphoglycerate mutase (iPGM) distinctively present in

59 ween the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearotherm

60 The B. subtilis strain with a high phosphoglycerate mutase level sporulated, and the spores

61 The phosphoglycerate mutase-like domain of Sts-1 (Sts-1(PGM)

62 of Leishmania mexicana cofactor-independent phosphoglycerate mutase (Lm iPGAM) crystallised with the

63 Knockout mutation of phosphoglycerate mutase or enolase resulted in a signifi

64 f glycolytic enzymes in Tregs and identified phosphoglycerate mutase (PGAM) as being differentially o

65 double labelled (15N,13C) monomeric, 23.7 kD phosphoglycerate mutase (PGAM) from Schizosaccharomyces

66 activity of 2,3-phosphoglycerate-independent phosphoglycerate mutase (PGAM), the enzyme that deviates

67 Here we report the interaction of Pak with phosphoglycerate mutase (PGAM)-B, an enzyme of the glyco

68 the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells

69 atase activity located within its C-terminal phosphoglycerate mutase (PGM) homology domain and key fo

70 the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first

71 The glycolytic enzyme phosphoglycerate mutase (PGM) is of utmost importance fo

72 Bacillus stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- an

73 fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM).

74 x proteins: TroA, TroB, TroC, TroD, TroR and Phosphoglycerate mutase (Pgm).

75 (GAPDH), phosphoglycerate kinase (PGK), and phosphoglycerate mutase (PGM).

76 Phosphoglycerate mutases (PGMs) catalyze the isomerizati

77 ogenase (GPDH), calcium-binding protein, and phosphoglycerate mutase were also identified.

78 mer-specific autophosphorylation of NME1 and phosphoglycerate mutase were used with immunoblotting an