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Literature summary extracted from

  • Maher, M.J.; Ghosh, M.; Grunden, A.M.; Menon, A.L.; Adams, M.W.; Freeman, H.C.; Guss, J.M.
    Structure of the prolidase from Pyrococcus furiosus (2004), Biochemistry, 43, 2771-2783.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.13.9 0.0025 ml of purified recombinant enzyme, 10 mg/ml, in 50 mM Tris-HCl, pH 8.5, 6.5-7.5% PEG 8000, 0.1 M magnesium acetate, hanging drop vapour diffusion, against 1.0 ml reservoir solution containing 13-15% PEG 8000, 0.2 M magnesium acetate, 50 mM Tris-HCl, pH 8.5, 20°C, 180 days, addition of solid (2S,3R)-3-amino-2-hydroxy-5-methyl-hexanoyl-proline and 15% 2-methyl-2,4-pentanediol for formation and crystallization of enzyme-inhibitor complex, X-ray structure determination and analysis at 2.0 A resolution of crystal form II Pyrococcus furiosus
3.4.13.9 native enzyme and in complex with inhibitor (2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-proline. One homodimer per asymmetric unit. Each subunit has two domains, the C-terminal domain includes the catalytic site centered on a dinuclear metal cluster Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.13.9 (2S,3R)-3-amino-2-hydroxy-5-methyl-hexanoyl-proline
-
 Pyrococcus furiosus
3.4.13.9 (2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-proline
-
 Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.13.9 Co2+ dinuclear metal cluster in the active site, binding of 2 Co2+ per subunit Pyrococcus furiosus
3.4.13.9 Zn2+ 2 Zn2+ bound to the subunit in the crystallized enzyme only replacing the Co2+ ions, binding structure via 5 coordinates Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.9 Pyrococcus furiosus
-
-
-
3.4.13.9 Pyrococcus furiosus P81535
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.13.9 590
-
 purified crystallized recombinant enzyme Pyrococcus furiosus
3.4.13.9 1300
-
 purified noncrystallized recombinant enzyme Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.9 Xaa-Pro + H2O
-
 Pyrococcus furiosus Xaa + Pro
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.13.9 dimer crystal structure, 2 subunits each with 2 domains, with the C-terminal domain bearing the active site Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
3.4.13.9 More enzyme belongs to the methionyl amino peptidase family M24, fomerly EC 3.4.3.7 Pyrococcus furiosus
3.4.13.9 Pfprol
-
 Pyrococcus furiosus
3.4.13.9 prolidase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.13.9 100
-
 assay at Pyrococcus furiosus