Phosphatase Subfamily PGAM - Revision history

Gerard: /* Catalytic activity */

2024-04-02T13:08:39Z

‎Catalytic activity

Gerard at 13:05, 2 April 2024

2024-04-02T13:05:22Z

Gerard at 21:50, 25 October 2016

2016-10-25T21:50:44Z

Mark at 20:21, 2 June 2015

2015-06-02T20:21:04Z

Mark at 17:57, 4 January 2015

2015-01-04T17:57:48Z

Mark: /* Evolution */

2015-01-04T17:57:29Z

‎Evolution

Mark: /* Evolution */

2015-01-04T17:54:09Z

‎Evolution

Mark: /* Catalytic activity */

2015-01-04T04:53:21Z

‎Catalytic activity

Mark: /* Catalytic activity */

2015-01-04T04:45:04Z

‎Catalytic activity

Mark: /* Catalytic activity */

2015-01-04T04:44:20Z

‎Catalytic activity

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 === Catalytic activity ===
 Human has four members:
-* [[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, promoting cancer cell proliferation and tumor growth. This is the mechanism behind oncogenic signalling to coordinate glycolysis and anabolic biosynthesis in cancer cells <cite>hitosugi12,hitosugi13</cite>. NAD+-dependent deacetylase Sirt1 deacetylates PGAM1 and attenuates catalytic activity <cite>hallows12</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). A muscle-specific form of PGAM <cite>tsujino93</cite>.
-* [[Phosphatase_Gene_PGAM2|PGAM2]]: phosphoglycerate mutase 2 (muscle). Glycolytic enzyme PGAM expressed in muscle <cite>tsujino93</cite>.
 * [[Phosphatase_Gene_PGAM4|PGAM4]] (aka PGAM3): phosphoglycerate mutase family member 4.
 === References ===

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HP|Fold HP]]: [[Phosphatase_Superfamily_HP|Superfamily HP]]:  [[Phosphatase_Family_HP1|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM|Subfamily PGAM]]
-PGAM subfamily mainly functions as glycolytic enzymes regulating intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate|2-phosphoglycerate]]. Human BPGM is a 2,3-bisphosphoglycerate mutase. They are found throughout most eukaryotes.
+PGAMs mainly function as glycolytic enzymes regulating intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate|2-phosphoglycerate]]. Human BPGM is a 2,3-bisphosphoglycerate mutase.
 === Evolution ===
-PGAM is found in most eukaryotic genomes with duplication in individual lineages. For instance, human has four members of PGAM subfamily, yeast has three. They emerged by independent duplication events.
+PGAM is found in most eukaryotic genomes with duplication in individual lineages. For instance, human has four PGAMs and yeast has three. They emerged by independent duplication events.
 === Domain ===
-PGAM has single domain, phosphatase domain of HP1 family.
+PGAM has single domain, a HP1-family phosphatase domain.
 === Catalytic activity ===

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 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HP|Fold HP]]: [[Phosphatase_Superfamily_HP|Superfamily HP]] (histidine phosphatase):  [[Phosphatase_Family_HP1|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM|Subfamily PGAM]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HP|Fold HP]]: [[Phosphatase_Superfamily_HP|Superfamily HP]]:  [[Phosphatase_Family_HP1|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM|Subfamily PGAM]]
 PGAM subfamily mainly functions as glycolytic enzymes regulating intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate|2-phosphoglycerate]]. Human BPGM is a 2,3-bisphosphoglycerate mutase. They are found throughout most eukaryotes.

← Older revision		Revision as of 20:21, 2 June 2015
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		+	__NOTOC__
	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HP\|Fold HP]]: [[Phosphatase_Superfamily_HP\|Superfamily HP]] (histidine phosphatase): [[Phosphatase_Family_HP1\|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM\|Subfamily PGAM]]		[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HP\|Fold HP]]: [[Phosphatase_Superfamily_HP\|Superfamily HP]] (histidine phosphatase): [[Phosphatase_Family_HP1\|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM\|Subfamily PGAM]]

← Older revision		Revision as of 17:57, 4 January 2015
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	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HP\|Fold HP]]: [[Phosphatase_Superfamily_HP\|Superfamily HP]] (histidine phosphatase): [[Phosphatase_Family_HP1\|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM\|Subfamily PGAM]]		[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HP\|Fold HP]]: [[Phosphatase_Superfamily_HP\|Superfamily HP]] (histidine phosphatase): [[Phosphatase_Family_HP1\|HP, branch1 family]]: [[Phosphatase_Subfamily_PGAM\|Subfamily PGAM]]
−

	PGAM subfamily mainly functions as glycolytic enzymes regulating intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate\|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate\|2-phosphoglycerate]]. Human BPGM is a 2,3-bisphosphoglycerate mutase. They are found throughout most eukaryotes.		PGAM subfamily mainly functions as glycolytic enzymes regulating intracellular levels of its substrate [[Phosphatase_Glossary#3-phosphoglycerate\|3-phosphoglycerate]] and product [[Phosphatase_Glossary#2-phosphoglycerate\|2-phosphoglycerate]]. Human BPGM is a 2,3-bisphosphoglycerate mutase. They are found throughout most eukaryotes.

← Older revision		Revision as of 04:53, 4 January 2015
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	* [[Phosphatase_Gene_PGAM2\|PGAM2]]: phosphoglycerate mutase 2 (muscle). Glycolytic enzyme PGAM expressed in muscle <cite>tsujino93</cite>.		* [[Phosphatase_Gene_PGAM2\|PGAM2]]: phosphoglycerate mutase 2 (muscle). Glycolytic enzyme PGAM expressed in muscle <cite>tsujino93</cite>.
	* [[Phosphatase_Gene_PGAM4\|PGAM4]] (aka PGAM3): phosphoglycerate mutase family member 4.		* [[Phosphatase_Gene_PGAM4\|PGAM4]] (aka PGAM3): phosphoglycerate mutase family member 4.
		+
		+	=== References ===
		+	<biblio>
		+	#wang04 pmid=15258155
		+	#wang06 pmid=23653202
		+	#hitosugi12 pmid=23153533
		+	#hitosugi13 pmid=23653202
		+	#hallows12 pmid=22157007
		+	#tsujino93 pmid=8447317
		+	</biblio>