Difference between revisions of "Phosphatase Subfamily PGAM"
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* [[Phosphatase_Gene_BPGM|BPGM]]: 2,3-bisphosphoglycerate mutase. Bisphosphoglycerate mutase is an erythrocyte-specific en- zyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3- bisphosphoglycerate <cite>wang04, wang06</cite>. | * [[Phosphatase_Gene_BPGM|BPGM]]: 2,3-bisphosphoglycerate mutase. Bisphosphoglycerate mutase is an erythrocyte-specific en- zyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3- bisphosphoglycerate <cite>wang04, wang06</cite>. | ||
| − | * [[Phosphatase_Gene_PGAM1|PGAM1]]: phosphoglycerate mutase 1 (brain). Glycolytic enzyme PGAM1 regulates anabolic biosynthesis by controlling intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate|2-phosphoglycerate]]. Y26 phosphorylation enhances PGAM1 activation through release of inhibitory E19 that blocks the active site, stabilising cofactor 2,3-bisphosphoglycerate binding and H11 phosphorylation. Y26 phosphorylation of PGAM1 is common in human cancer cells and contributes to regulation of 3-phosphoglycerate and 2-phosphoglycerate levels, promoting cancer cell proliferation and tumour growth. This is the mechanism behind oncogenic signalling coordinates glycolysis and anabolic biosynthesis in cancer cells <cite>hitosugi12,hitosugi13</cite>. | + | * [[Phosphatase_Gene_PGAM1|PGAM1]]: phosphoglycerate mutase 1 (brain). Glycolytic enzyme PGAM1 regulates anabolic biosynthesis by controlling intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate|2-phosphoglycerate]]. Y26 phosphorylation enhances PGAM1 activation through release of inhibitory E19 that blocks the active site, stabilising cofactor 2,3-bisphosphoglycerate binding and H11 phosphorylation. Y26 phosphorylation of PGAM1 is common in human cancer cells and contributes to regulation of 3-phosphoglycerate and 2-phosphoglycerate levels, promoting cancer cell proliferation and tumour growth. This is the mechanism behind oncogenic signalling coordinates glycolysis and anabolic biosynthesis in cancer cells <cite>hitosugi12,hitosugi13</cite>. NAD+-dependent deacetylase Sirt1 deacetylates phosphoglycerate mutase-1 (PGAM1) and attenuates catalytic activity <cite>hallows12</cite>. |
| − | * [[Phosphatase_Gene_PGAM2|PGAM2]]: phosphoglycerate mutase 2 (muscle) | + | * [[Phosphatase_Gene_PGAM2|PGAM2]]: phosphoglycerate mutase 2 (muscle). Glycolytic enzyme PGAM expressed in muscle. |
| − | * [[Phosphatase_Gene_PGAM4|PGAM4]] (aka PGAM3): phosphoglycerate mutase family member 4 | + | * [[Phosphatase_Gene_PGAM4|PGAM4]] (aka PGAM3): phosphoglycerate mutase family member 4. |
Revision as of 04:44, 4 January 2015
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): HP, branch1 family: Subfamily PGAM
Evolution
Domain
PGAM has single domain, phosphatase domain of HP1 family.
Catalytic activity
Human has four members:
- BPGM: 2,3-bisphosphoglycerate mutase. Bisphosphoglycerate mutase is an erythrocyte-specific en- zyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3- bisphosphoglycerate [1, 2].
- PGAM1: phosphoglycerate mutase 1 (brain). Glycolytic enzyme PGAM1 regulates anabolic biosynthesis by controlling intracellular levels of its substrate 3-phosphoglycerate and product 2-phosphoglycerate. Y26 phosphorylation enhances PGAM1 activation through release of inhibitory E19 that blocks the active site, stabilising cofactor 2,3-bisphosphoglycerate binding and H11 phosphorylation. Y26 phosphorylation of PGAM1 is common in human cancer cells and contributes to regulation of 3-phosphoglycerate and 2-phosphoglycerate levels, promoting cancer cell proliferation and tumour growth. This is the mechanism behind oncogenic signalling coordinates glycolysis and anabolic biosynthesis in cancer cells [3, 4]. NAD+-dependent deacetylase Sirt1 deacetylates phosphoglycerate mutase-1 (PGAM1) and attenuates catalytic activity [5].
- PGAM2: phosphoglycerate mutase 2 (muscle). Glycolytic enzyme PGAM expressed in muscle.
- PGAM4 (aka PGAM3): phosphoglycerate mutase family member 4.
