| + |
PGM2 | up-regulates quantity 
chemical modification
|
D-ribofuranose 5-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267076 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17804405 |
Phosphopentomutase catalyzes the conversion of the nucleoside breakdown products ribose 1-phosphate and deoxyribose 1-phosphate to the corresponding 5-phosphopentoses. The role of phosphopentomutase is to utilize ribose 1-phosphate and deoxyribose 1-phosphate, which are formed by purine nucleoside phosphorylase and uridine phosphorylase. Using catalytic efficiency as a criterion, PGM2 acted more than 10-fold better as a phosphopentomutase (both on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a phosphoglucomutase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
PGM2 | down-regulates quantity 
chemical modification
|
alpha-D-ribose 1-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267075 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17804405 |
Phosphopentomutase catalyzes the conversion of the nucleoside breakdown products ribose 1-phosphate and deoxyribose 1-phosphate to the corresponding 5-phosphopentoses. The role of phosphopentomutase is to utilize ribose 1-phosphate and deoxyribose 1-phosphate, which are formed by purine nucleoside phosphorylase and uridine phosphorylase. Using catalytic efficiency as a criterion, PGM2 acted more than 10-fold better as a phosphopentomutase (both on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a phosphoglucomutase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
PGM2 | up-regulates quantity
chemical modification
|
alpha-D-glucose 6-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267934 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32898648 |
Human PGM1 deficiency is an inborn error of metabolism (OMIM: 614921), affecting cellular glucose homeostasis, the storage of glucose as glycogen, and the N-glycosylation of proteins. Like other PGM enzymes, the human protein catalyzes the Mg2+-dependent interconversion of glucose 1-phosphate (G1P) and glucose 6-phosphate (G6P). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis, Glycogenolysis, Pentose phosphate pathway |
| + |
PGM2 | up-regulates quantity
chemical modification
|
alpha-D-glucose 1-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267933 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32898648 |
Human PGM1 deficiency is an inborn error of metabolism (OMIM: 614921), affecting cellular glucose homeostasis, the storage of glucose as glycogen, and the N-glycosylation of proteins. Like other PGM enzymes, the human protein catalyzes the Mg2+-dependent interconversion of glucose 1-phosphate (G1P) and glucose 6-phosphate (G6P). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis, Glycogenolysis |
| + |
PGM2 | down-regulates quantity
chemical modification
|
alpha-D-glucose 1-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268115 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32898648 |
Human PGM1 deficiency is an inborn error of metabolism (OMIM: 614921), affecting cellular glucose homeostasis, the storage of glucose as glycogen, and the N-glycosylation of proteins. Like other PGM enzymes, the human protein catalyzes the Mg2+-dependent interconversion of glucose 1-phosphate (G1P) and glucose 6-phosphate (G6P). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis, Glycogenolysis |
| + |
PGM2 | down-regulates quantity
chemical modification
|
alpha-D-glucose 6-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268116 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32898648 |
Human PGM1 deficiency is an inborn error of metabolism (OMIM: 614921), affecting cellular glucose homeostasis, the storage of glucose as glycogen, and the N-glycosylation of proteins. Like other PGM enzymes, the human protein catalyzes the Mg2+-dependent interconversion of glucose 1-phosphate (G1P) and glucose 6-phosphate (G6P). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis, Glycogenolysis, Pentose phosphate pathway |
| + |
PGM2 | up-regulates quantity
chemical modification
|
2-deoxy-D-ribose 5-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267095 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17804405 |
Biochemical characterization of phosphoglucomutase (PGM) isozymes indicated that one of them, designated PGM2 in man (PGM1 in mouse) was more active as a phosphopentomutase than as a phosphoglucomutase, whereas mammalian PGM1 (equivalent to PGM2 in mouse) has a phosphopentomutase activity representing only about 0.2% of its phosphoglucomutase activity. Phosphopentomutase catalyzes the conversion of the nucleoside breakdown products ribose 1-phosphate and deoxyribose 1-phosphate to the corresponding 5-phosphopentoses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
PGM2 | down-regulates quantity
chemical modification
|
2-deoxy-alpha-D-ribose 1-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267094 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17804405 |
Biochemical characterization of phosphoglucomutase (PGM) isozymes indicated that one of them, designated PGM2 in man (PGM1 in mouse) was more active as a phosphopentomutase than as a phosphoglucomutase, whereas mammalian PGM1 (equivalent to PGM2 in mouse) has a phosphopentomutase activity representing only about 0.2% of its phosphoglucomutase activity. Phosphopentomutase catalyzes the conversion of the nucleoside breakdown products ribose 1-phosphate and deoxyribose 1-phosphate to the corresponding 5-phosphopentoses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
3.0
PGM2
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