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Literature summary extracted from

  • Theriot, C.M.; Tove, S.R.; Grunden, A.M.
    Biotechnological applications of recombinant microbial prolidases (2009), Adv. Appl. Microbiol., 68, 99-132.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.13.9 analysis applications using prolidase to detoxify organophosphorous compounds nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection Pyrococcus furiosus
3.4.13.9 biotechnology the enzyme is of particular interest because it can be used in many biotechnological applications Pyrococcus furiosus
3.4.13.9 degradation advantages of using Alteromonas recombinant prolidase in biodecontamination foams due to its high activity against G-type nerve agents, such as soman and sarin Alteromonas sp.
3.4.13.9 degradation prolidase is able to degrade toxic organophosphorus compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman. Applications using prolidase to detoxify organophosphorous nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection Pyrococcus furiosus
3.4.13.9 diagnostics prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy Homo sapiens
3.4.13.9 drug development prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy Homo sapiens
3.4.13.9 food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Pyrococcus furiosus
3.4.13.9 food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Lactococcus lactis
3.4.13.9 food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Lacticaseibacillus casei
3.4.13.9 medicine Recombinant human prolidase is used for enzyme replacement therapy in prolidase deficiency Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.9 expression in Escherichia coli Homo sapiens
3.4.13.9 expression in Escherichia coli Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.13.9 Co2+ activates Cavia porcellus
3.4.13.9 Co2+ activates Homo sapiens
3.4.13.9 Co2+ activates Lacticaseibacillus casei
3.4.13.9 Co2+ activates Stenotrophomonas maltophilia
3.4.13.9 Co2+ activates, preferred metal ion Lactococcus lactis
3.4.13.9 Co2+ highly activating, one Co2+ per enzyme subunit Pyrococcus furiosus
3.4.13.9 Fe2+ best activating divalent ion Pyrococcus furiosus
3.4.13.9 Mn2+ activates Cavia porcellus
3.4.13.9 Mn2+ activates Pyrococcus furiosus
3.4.13.9 Mn2+ activates Lactococcus lactis
3.4.13.9 Mn2+ requires divalent cations for activity, most active with manganese Homo sapiens
3.4.13.9 Mn2+ requires divalent cations for activity, most active with manganese Lacticaseibacillus casei
3.4.13.9 Mn2+ requires divalent cations for activity, most active with manganese Stenotrophomonas maltophilia
3.4.13.9 Mn2+ requires divalent cations for activity, most active with manganese Alteromonas sp.
3.4.13.9 additional information the enzyme requires divalent cations for activity Lactococcus lactis
3.4.13.9 additional information OPAA-2 has a conserved binuclear metal center Alteromonas sp.
3.4.13.9 additional information the enzyme contains a dinuclear metal center bridged by a water molecule or hydroxide ion. The metal cluster is essential for the activation of catalysis. It functions to activate a nucleophile for the reaction, as well as participating in substrate binding and stabilizing the transition state. The dipeptidase is maximally active with the addition of the divalent cations Co2+ and Mn2+ and it cannot be substituted with other divalent cations, i.e Mg2+, Ca2+, Fe2+, Ni2+, Cu2+, or Zn2+, under aerobic conditions Pyrococcus furiosus
3.4.13.9 Zn2+ interaction with amino acid residues D209, D220, H284, E313 and E327, overview Pyrococcus furiosus
3.4.13.9 Zn2+ requires divalent cations for activity, most active with zinc Lactobacillus delbrueckii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.13.9 39400
-
 2 * 39400, structure-function relationship, overview. The enzyme shows a pita-bread fold that encompasses a highly conserved metal center and substrate-binding pocket that is located in the enzymes C-terminal domain Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.13.9 additional information Homo sapiens prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position ?
-
 ?
3.4.13.9 additional information Pyrococcus furiosus prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.9 Alteromonas sp.
-
-
-
3.4.13.9 Alteromonas sp. JD6.5
-
-
-
3.4.13.9 Cavia porcellus
-
-
-
3.4.13.9 Homo sapiens
-
-
-
3.4.13.9 Lacticaseibacillus casei
-
-
-
3.4.13.9 Lacticaseibacillus casei IFPL 731
-
-
-
3.4.13.9 Lactobacillus delbrueckii
-
 gene pepQ
-
3.4.13.9 Lactococcus lactis
-
-
-
3.4.13.9 Pyrococcus furiosus
-
-
-
3.4.13.9 Stenotrophomonas maltophilia
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.13.9 hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro mechanism of substrate specificity and catalysis, detailed overview Pyrococcus furiosus
a
3.4.13.9 hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro mechanism of substrate specificity and catalysis, overview Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.13.9 brain
-
 Cavia porcellus
-
3.4.13.9 breast
-
 Homo sapiens
-
3.4.13.9 breast cancer cell increased prolidase activity in breast cancer tissue Homo sapiens
-
3.4.13.9 connective tissue
-
 Homo sapiens
-
3.4.13.9 melanoma cell high expression level Homo sapiens
-
3.4.13.9 additional information optimal growth at 100°C Pyrococcus furiosus
-

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 additional information
-
 activities of strain JD6.5 enzyme in the presence or absence of various biodegradeable and water-soluble wetting agents, degreasers, or foams, overview Alteromonas sp.
3.4.13.9 10
-
 at 30°C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP Homo sapiens
3.4.13.9 30
-
 at 55°C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP Pyrococcus furiosus
3.4.13.9 1950
-
-
 Alteromonas sp.

Storage Stability

EC Number Storage Stability Organism
3.4.13.9 37°C, recombinant enzyme from expression in Escherichia coli, stable for 6 days Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.9 Met-Pro + H2O
-
 Pyrococcus furiosus Met + Pro
-
 ?
3.4.13.9 additional information prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position Homo sapiens ?
-
 ?
3.4.13.9 additional information prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position Pyrococcus furiosus ?
-
 ?
3.4.13.9 additional information OPAA-2 can hydrolyze organophosphorus acid nerve agents, such as sarin and soman. OPAA-2 has been reclassified as a prolidase because it can also efficiently hydrolyze X-Pro dipeptides. The enzyme OPAA-2 shows activity with P-F, P-C and P-O bonds. It can also preferentially cleave the dipeptides Leu-Pro and Ala-Pro and is specific for dipeptides with proline in the C-terminal position, but shows no activity with the substrates Pro-Leu and Pro-Gly Alteromonas sp. ?
-
 ?
3.4.13.9 additional information Pfprol has a narrow substrate specificity, only hydrolyzing dipeptides with a proline in the C-terminus and nonpolar amino acids, Leu, Met, Val, Phe, or Ala, in the N-terminal position. Pfprol cannot cleave dipeptides with proline in the N-terminus. Substrate binding, structure-function relationship, overview. No activity on organophosphorus nerve agents sarin, cyclosarin, and soman, but with diisopropyl phosphorofluoridate Pyrococcus furiosus ?
-
 ?
3.4.13.9 additional information the enzyme from guinea pig brain can also cleave substrates without a prolyl residue Cavia porcellus ?
-
 ?
3.4.13.9 additional information the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue Lacticaseibacillus casei ?
-
 ?
3.4.13.9 additional information the enzyme is also active with diisopropyl phosphorofluoridate, an organophosphorus nerve reagent Homo sapiens ?
-
 ?
3.4.13.9 additional information the enzyme only hydrolyzes dipeptides with a proline in the C-terminus and cannot cleave dipeptides with proline in the N-terminus Lactobacillus delbrueckii ?
-
 ?
3.4.13.9 additional information OPAA-2 can hydrolyze organophosphorus acid nerve agents, such as sarin and soman. OPAA-2 has been reclassified as a prolidase because it can also efficiently hydrolyze X-Pro dipeptides. The enzyme OPAA-2 shows activity with P-F, P-C and P-O bonds. It can also preferentially cleave the dipeptides Leu-Pro and Ala-Pro and is specific for dipeptides with proline in the C-terminal position, but shows no activity with the substrates Pro-Leu and Pro-Gly Alteromonas sp. JD6.5 ?
-
 ?
3.4.13.9 additional information the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue Lacticaseibacillus casei IFPL 731 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.13.9 dimer
-
 Homo sapiens
3.4.13.9 dimer
-
 Stenotrophomonas maltophilia
3.4.13.9 homodimer 2 * 39400, structure-function relationship, overview. The enzyme shows a pita-bread fold that encompasses a highly conserved metal center and substrate-binding pocket that is located in the enzyme's C-terminal domain Pyrococcus furiosus
3.4.13.9 monomer
-
 Lactococcus lactis
3.4.13.9 monomer
-
 Lacticaseibacillus casei
3.4.13.9 monomer
-
 Alteromonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.4.13.9 More prolidase belongs to a subclass of metallopeptidases that contain a dinuclear active-site metal cluster, and further into a smaller class of metalloenzymes known as the pita-bread enzymes Homo sapiens
3.4.13.9 More prolidase belongs to a subclass of metallopeptidases, that contain a dinuclear active-site metal cluster, with a smaller class of metalloenzymes known as the pita-bread enzymes Pyrococcus furiosus
3.4.13.9 OPAA-2
-
 Alteromonas sp.
3.4.13.9 organophosphorus acid anhydrolase
-
 Alteromonas sp.
3.4.13.9 PepQ
-
 Lactobacillus delbrueckii
3.4.13.9 Pfprol
-
 Pyrococcus furiosus
3.4.13.9 prolidase
-
 Cavia porcellus
3.4.13.9 prolidase
-
 Homo sapiens
3.4.13.9 prolidase
-
 Pyrococcus furiosus
3.4.13.9 prolidase
-
 Lactococcus lactis
3.4.13.9 prolidase
-
 Lacticaseibacillus casei
3.4.13.9 prolidase
-
 Lactobacillus delbrueckii
3.4.13.9 prolidase
-
 Stenotrophomonas maltophilia
3.4.13.9 prolidase
-
 Alteromonas sp.
3.4.13.9 proline iminopeptidase
-
 Homo sapiens
3.4.13.9 proline iminopeptidase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.13.9 100
-
 with Co2+ and substrate Met-Pro Pyrococcus furiosus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.13.9 50 100 hardly active below 50°C, optimal activity at 100°C Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.13.9 50
-
 little activity remaining after 6 h Pyrococcus furiosus
3.4.13.9 80
-
 loss of 50% activity after 6 h Pyrococcus furiosus
3.4.13.9 100
-
 native Pfprol shows no loss of activity after incubation for 12 h at 100°C, while the recombinant prolidase produced in Escherichia coli exhibits a 50% loss of activity after incubation for 6 h at 100°C Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.13.9 7
-
 with Co2+ and substrate Met-Pro Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
3.4.13.9 malfunction prolidase deficiency is a rare autosomal recessive disorder that affects the connective tissue. Symptoms of prolidase deficiency include skin lesions, mental retardation and recurrent respiratory infections. Prolidase is linked to collagen metabolism and is associated with melanoma. Prolidase is essential for collagen breakdown and the lack of this enzyme results in serious skin abnormalities. While an increase in prolidase activity and a decrease in collagen in breast cancer tissue may cause increased cancer risk. Recombinant human prolidase is used for enzyme replacement therapy Homo sapiens
3.4.13.9 metabolism the enzyme is important in the collagen metabolism, overview Homo sapiens
3.4.13.9 physiological function OPAA-2 is active in detoxification of organophosphorus compounds, the nerve agents GB, sarin or O-isopropyl methylphosphonofluoridate, VX and blister agent HD, a sulfur mustard, overview Alteromonas sp.