cd03089

PMM_PGM

CDD entry
Member databaseCDD
CDD typedomain
Short namePMM_PGM
Setphosphohexomutase

Description

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
[7, 5, 6, 3, 2, 1, 8, 4]

References

1.Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Regni C, Tipton PA, Beamer LJ. Structure 10, 269-79, (2002). View articlePMID: 11839312

2.Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Regni C, Naught L, Tipton PA, Beamer LJ. Structure 12, 55-63, (2004). View articlePMID: 14725765

3.Evolutionary trace analysis of the alpha-D-phosphohexomutase superfamily. Shackelford GS, Regni CA, Beamer LJ. Protein Sci. 13, 2130-8, (2004). View articlePMID: 15238632

4.A phylogenetic approach to the identification of phosphoglucomutase genes. Whitehouse DB, Tomkins J, Lovegrove JU, Hopkinson DA, McMillan WO. Mol. Biol. Evol. 15, 456-62, (1998). View articlePMID: 9549096

5.The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme. Regni C, Schramm AM, Beamer LJ. J. Biol. Chem. 281, 15564-71, (2006). View articlePMID: 16595672

6.Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Akutsu J, Zhang Z, Tsujimura M, Sasaki M, Yohda M, Kawarabayasi Y. J Biochem 138, 159-66, (2005). PMID: 16091590

7.Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Regni C, Shackelford GS, Beamer LJ. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 722-6, (2006). View articlePMID: 16880541

8.Functional diversity of the phosphoglucomutase superfamily: structural implications. Levin S, Almo SC, Satir BH. Protein Eng. 12, 737-46, (1999). View articlePMID: 10506283

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