spacer

Overview for MACiE Entry M0194

Version history

General Information

EC Number: 5.4.2.8 (A member of the Isomerases, Intramolecular transferases, Phosphotransferases (phosphomutases))

Enzyme Name: phosphomannomutase/phosphoglucomutase

Biological Species: Pseudomonas aeruginosa (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P26276 - Phosphomannomutase/phosphoglucomutase

Representative PDB Code: 1p5d - ENZYME-LIGAND COMPLEX OF P. AERUGINOSA PMM/PGM (Resolution = 1.60 Å).

Catalytic CATH Codes:

  • 3.40.120.10 - Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of D-mannose 6-phosphate

right arrow

Image of D-mannose 1-phosphate

D-mannose 6-phosphate
C00275
CHEBI:17369
D-mannose 1-phosphate
C00636
CHEBI:4210

Overall Comment: This enzyme catalyse both EC reactions 5.4.2.8 and 5.4.2.2 with equal efficiency. The reaction requires a phosphorylated enzyme and an activator glucose 1,6-biphosphate to maintain the enzyme in its phosphorylated state [1]. The crystal structures for this enzyme contain Zn(II) rather than Mg(II) in the active site to render them catalytically inactive [3].


View similar reactions


Stepwise Description of the Reaction

Step 1D-mannose 6-phosphate attacks the phosphorylated Ser108 in a nucleophilic substitution, resulting in phosphorylation of the 1 position.
Step 2The 1,6-biphosphate rotates in the active site before Ser108 attacks the 6 phosphate in a nucleophilic substitution reaction, resulting in regeneration of the phosphorylated serine and the D-mannose 1-phosphate product.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Arg 20 X Side Chain
Sep 108 X Post-translationally modified residue
His 109 X Side Chain
Lys 118 X Side Chain
Arg 247 X Side Chain
His 329 X Side Chain

Metal Cofactors for M0194

Type Het group Number Chain
magnesium ZN 500 x Overview

References

  1. L. E. Naught et al. (2003), Biochemistry, 42, 9946-9951. Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
    Medline: 12924943
  2. L. E. Naught et al. (2001), Arch. Biochem. Biophys., 396, 111-118. Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
    Medline: 11716469
  3. C. Regni et al. (2004), Structure, 12, 55-63. Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
    Medline: 14725765

Homologue information for M0194 (1p5d)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

GOA logo
magnesium ion binding (molecular function)
catalytic activity (molecular function)
phosphoglucomutase activity (molecular function)
phosphomannomutase activity (molecular function)
carbohydrate metabolic process (biological process)
metabolic process (biological process)
lipopolysaccharide biosynthetic process (biological process)
isomerase activity (molecular function)
intramolecular transferase activity, phosphotransferases (molecular function)
alginic acid biosynthetic process (biological process)
metal ion binding (molecular function)
spacer
spacer