Literature summary for 5.4.2.11 extracted from

Walter, R.A.; Nairn, J.; Duncan, D.; Price, N.C.; Kelly, S.M.; Rigden, D.J.; Fothergill-Gilmore, L.A.
The role of the C-terminal region in phosphoglycerate mutase (1999), Biochem. J., 337, 89-95.

No PubMed abstract available

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Activating Compound

Activating Compound	Comment	Organism	Structure
2,3-bisphosphoglycerate	-	Saccharomyces cerevisiae
2-phosphoglycollate	18-20fold activation of phosphatase activity	Saccharomyces cerevisiae
2-phosphoglycollate	2.3fold activation of phosphatase activity	Schizosaccharomyces pombe
2-phosphohydroxypyruvate	30fold activation of phosphatase activity	Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment)	Organism
-	Schizosaccharomyces pombe
expression in Saccharomyces cerevisiae	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
L245G	39% of wild-type mutase activity, 111% of wild-type phosphatase activity	Saccharomyces cerevisiae
L245G/L246G	105% of wild-type mutase activity, 111% of wild-type phosphatase activity	Saccharomyces cerevisiae
L246G	98% of wild-type mutase activity, 122% of wild-type phosphatase activity	Saccharomyces cerevisiae

General Stability

General Stability	Organism
loss of 45% of mutase activity after treatment with thermolysin	Saccharomyces cerevisiae
relatively resistant to short periods of treatment with thermolysin, both mutase and phosphatase activity decline at the same rate, approx. 40% loss of activity after 120 min treatment with thermolysin	Schizosaccharomyces pombe

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.22	-	3-phospho-D-glycerate	phosphatase activity	Saccharomyces cerevisiae
0.4	-	3-phospho-D-glycerate	L245G mutant	Saccharomyces cerevisiae
0.47	-	3-phospho-D-glycerate	mutase activity	Saccharomyces cerevisiae
0.58	-	3-phosphoglycerate	mutase activity	Schizosaccharomyces pombe
0.63	-	3-phospho-D-glycerate	L246G mutant	Saccharomyces cerevisiae
1.43	-	3-phospho-D-glycerate	L245G/L246G double mutant	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27000	-	4 * 27000, SDS-PAGE	Saccharomyces cerevisiae
27000	-	4 * 27000, SDS-PAGE	Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-phospho-D-glycerate	Schizosaccharomyces pombe	-	3-phospho-D-glycerate	-	r
2-phospho-D-glycerate + 2,3-bisphosphoglycerate	Saccharomyces cerevisiae	-	3-phospho-D-glycerate + 2,3-bisphosphoglycerate	-	r

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-
Schizosaccharomyces pombe	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant PGAM	Schizosaccharomyces pombe
recpmbinant PGAM	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phospho-D-glycerate	-	Schizosaccharomyces pombe	3-phospho-D-glycerate	-	r
2-phospho-D-glycerate + 2,3-bisphosphoglycerate	-	Saccharomyces cerevisiae	3-phospho-D-glycerate + 2,3-bisphosphoglycerate	-	r
2-phospho-D-glycerate + 2,3-bisphosphoglycerate	phosphorylated PGAM also has low levels, i.e. 0.002% of mutase activity, of phosphatase activity	Saccharomyces cerevisiae	3-phospho-D-glycerate + 2,3-bisphosphoglycerate	-	r
3-Phosphoglycerate	-	Schizosaccharomyces pombe	2-Phosphoglycerate	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 27000, SDS-PAGE	Saccharomyces cerevisiae
tetramer	4 * 27000, SDS-PAGE	Schizosaccharomyces pombe

Synonyms

Synonyms	Comment	Organism
PGAM	-	Saccharomyces cerevisiae
PGAM	-	Schizosaccharomyces pombe

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0009	-	3-phospho-D-glycerate	phosphatase activity	Saccharomyces cerevisiae
0.02	-	3-phospho-D-glycerate	phosphatase activity	Schizosaccharomyces pombe
82	-	3-phospho-D-glycerate	mutase activity	Schizosaccharomyces pombe
530	-	3-phospho-D-glycerate	mutase activity	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
2,3-bisphosphoglycerate	required to prime the reaction in an initial phosphorylation step	Schizosaccharomyces pombe

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Release 2023.1 (January 2023)