5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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For detailed information about phosphoglycerate mutase (2,3-diphosphoglycerate-dependent), go to the full flat file.

Reaction

Synonyms

2,3-bisphosphoglycerate-dependent PGAM, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, alpha-PGAM, B-type PGM, cofactor-dependent phosphoglycerate mutase, dPGAM, DPGM, dPGM-B, EC 2.7.5.3, EC 3.1.3.13, EC 5.4.2.1, EntD, PGAM, PGAM1, PGAM2, PGM, phosphoglycerate mutase, phosphoglycerate mutase 1, phosphoglycerate mutase type B, Phosphoglyceromutase, Rv3214, ScPGM, SSO2236, Sts-1

ECTree

     5 Isomerases

         5.4 Intramolecular transferases

             5.4.2 Phosphotransferases (phosphomutases)

                5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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30	Activating Compound
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Reaction

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Reaction on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

2-phospho-D-glycerate = 3-phospho-D-glycerate

7 entries

[enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 2/3-phospho-D-glycerate

(1a)

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[enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 3-phospho-D-glycerate

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[enzyme]-Ntau-phospho-L-histidine + 2-phospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate

(1b)

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[enzyme]-Ntau-phospho-L-histidine + 2/3-bisphospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate

(1d)

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2-phospho-D-glycerate = 3-phospho-D-glycerate

mechanism: after the active site His-8 is phosphorylated by the cofactor 2,3-diphosphoglycerate a substrate molecule binds. Subsequently a phospho-transfer takes place via a ping-pong-mechanism. After release of the product the enzyme remains phosphorylated and catalytically competent

Saccharomyces cerevisiae

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3231

2-phospho-D-glycerate = 3-phospho-D-glycerate

ping-pong mechanism via a phosphorylated His-intermediate

Saccharomyces cerevisiae

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3240

2-phospho-D-glycerate = 3-phospho-D-glycerate

ping-pong mechanism via a phosphorylated His-intermediate

Oryctolagus cuniculus

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3240

2-phospho-D-glycerate = 3-phospho-D-glycerate

ping-pong or phosphoenzyme mechanism

Homo sapiens

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661261

2-phospho-D-glycerate = 3-phospho-D-glycerate

overall reaction

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2-phospho-D-glycerate = 3-phospho-D-glycerate

mechanism of BPGM begins with an unphosphorylated enzyme, the active site histidine of which performs a nucleophilic SN2 attack on the 1,3-bisphosphoglycerate substrate to produce phosphohistidine and 3-phosphoglycerate. The 2'-hydroxyl group then performs a second nucleophilic attack that transfers the phosphate from the active site histidine to the substrate, forming 2,3-bisphosphoglycerate

Burkholderia pseudomallei

Q3JWH7

726607

2-phospho-D-glycerate = 3-phospho-D-glycerate

mechanism of BPGM begins with an unphosphorylated enzyme, the active site histidine of which performs a nucleophilic SN2 attack on the 1,3-bisphosphoglycerate substrate to produce phosphohistidine and 3-phosphoglycerate. The 2'-hydroxyl group then performs a second nucleophilic attack that transfers the phosphate from the active site histidine to the substrate, forming 2,3-bisphosphoglycerate

Burkholderia pseudomallei 1710b

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