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The structural perturbation resulting from mutation of this single amino acid reveals the molecular mechanism underlying PGM1 deficiency in these missense variants.
Homozygous mutation in the PGM1 gene is associated with PGM1 deficiency.
analysis of the structural basis of PGM1 enzyme dysfunction in PGM1 deficiency
both PGM1 protein misfolding and catalytic impairment may play a role in PGM1 deficiency
PGM1 is required for sustained cell growth during nutritional changes
Phosphoglucomutase 1 deficiency, previously identified as a glycogenosis, is also a congenital disorder of glycosylation.
The analysis involved the data on nine polymorphic codominant loci: HP, GC, TF, PI, PGM1, GLO1 (show GLO1 Proteins), C3, ACP1 (show ACP1 Proteins), and ESD (show ESD Proteins). The loci were selected by significance of differences in genotype frequencies between tuberculosis patients and healthy controls
cell signaling kinase Pak1 (show PAK1 Proteins) is a novel regulator of glucose metabolism through its phosphorylation and regulation of PGM (show Vcan Proteins) activity.
Results report a novel human protein, calphoglin, which activates inorganic pyrophosphatase (IPP) and enhances phosphoglucomutase activity through the activated IPP.
During extrauterine life, females carrying the PGM1*2 allele are relatively protected from extreme body mass increase, and during intrauterine life, PGM1*2/*2 homozygotes show a tendency to low body mass increase.
Growth reduction in the pgm (show Vcan Proteins) mutant is largely caused by exaggerated root respiration, but not by leaf respiration.
The focus of this report is the analysis of gravitropic responses in lateral roots of wild-type background and pgm-1 mutants.
pgm-1 roots respond to gravity at one-third the rate of wild-type (WT) roots.
Sucrose-inducible genes are upregulated in pgm (show Vcan Proteins) leaves at the end of a light treatment, when soluble sugars levels are higher than in the wild type.
Data indicate that the phosphoglucomutase 1 (PGM1) pattern of expression changes during skeletal muscle development.
The protein encoded by this gene is an isozyme of phosphoglucomutase (PGM) and belongs to the phosphohexose mutase family. There are several PGM isozymes, which are encoded by different genes and catalyze the transfer of phosphate between the 1 and 6 positions of glucose. In most cell types, this PGM isozyme is predominant, representing about 90% of total PGM activity. In red cells, PGM2 is a major isozyme. This gene is highly polymorphic. Mutations in this gene cause glycogen storage disease type 14. Alternativley spliced transcript variants encoding different isoforms have been identified in this gene.
, glucose phosphomutase 1
, hypothetical protein
, glucose phosphomutase 2
, phosphoglucomutase 2
, phosphoglucomutase 1
, phosphoglucomutase isoform1
, Glucose phosphomutase 1