Literature summary for 3.4.13.9 extracted from

Willingham, K.; Maher, M.J.; Grunden, A.M.; Ghosh, M.; Adams, M.W.; Freeman, H.C.; Guss, J.M.
Crystallization and characterization of the prolidase from Pyrococcus furiosus (2001), Acta Crystallogr. Sect. D, 57, 428-430.

Crystallization (Commentary)

Crystallization (Comment)	Organism
10 mg/ml purified recombinant enzyme in 0.25 M MOPS, pH 7.0, hanging drop vapour diffusion method, 0.0025 ml with equal volume of precipitant solution containing PEG 8000 or PEG 4000, best in 0.1 M Tris-HCl, pH 8.5, 0.2 M magnesium acetate, 13-15% PEG 8000, room temperature, after 1 day cyrstals of form I appear, after 6 months crystals of form II appear, X-ray structure determination and analysis at 3.2 A and 1.95 A resolution for Form I and II, respectively, cryoprotection with solution containing 2-methyl-2,4-pentanediol	Pyrococcus furiosus

Crystallization (Comment)

Organism

10 mg/ml purified recombinant enzyme in 0.25 M MOPS, pH 7.0, hanging drop vapour diffusion method, 0.0025 ml with equal volume of precipitant solution containing PEG 8000 or PEG 4000, best in 0.1 M Tris-HCl, pH 8.5, 0.2 M magnesium acetate, 13-15% PEG 8000, room temperature, after 1 day cyrstals of form I appear, after 6 months crystals of form II appear, X-ray structure determination and analysis at 3.2 A and 1.95 A resolution for Form I and II, respectively, cryoprotection with solution containing 2-methyl-2,4-pentanediol

Pyrococcus furiosus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cobalt	2 atoms per subunit are required for optimum activity	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystal structure	Pyrococcus furiosus

Synonyms

Synonyms	Comment	Organism
More	enzyme belongs to the methionyl amino peptidase family M24, fomerly EC 3.4.3.7	Pyrococcus furiosus
prolidase	-	Pyrococcus furiosus
proline-specific amino dipeptidase	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)