Literature summary 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)

EC Number	Crystallization (Comment)	Organism
3.4.13.9	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

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

Organism

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

Subunits

EC Number	Subunits	Comment	Organism
3.4.13.9	dimer	crystal structure	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	prolidase	-	Pyrococcus furiosus
3.4.13.9	proline-specific amino dipeptidase	-	Pyrococcus furiosus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)