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Literature summary for 3.4.13.9 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
Search for more literature for 3.4.13.9

Application

Application Comment Organism
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
biotechnology the enzyme is of particular interest because it can be used in many biotechnological applications Pyrococcus furiosus
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.
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
diagnostics prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy Homo sapiens
drug development prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy Homo sapiens
food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Pyrococcus furiosus
food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Lactococcus lactis
food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture Lacticaseibacillus casei
medicine Recombinant human prolidase is used for enzyme replacement therapy in prolidase deficiency Homo sapiens

Cloned(Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Cavia porcellus
Co2+ activates Homo sapiens
Co2+ activates Lacticaseibacillus casei
Co2+ activates Stenotrophomonas maltophilia
Co2+ activates, preferred metal ion Lactococcus lactis
Co2+ highly activating, one Co2+ per enzyme subunit Pyrococcus furiosus
Fe2+ best activating divalent ion Pyrococcus furiosus
Mn2+ activates Cavia porcellus
Mn2+ activates Pyrococcus furiosus
Mn2+ activates Lactococcus lactis
Mn2+ requires divalent cations for activity, most active with manganese Homo sapiens
Mn2+ requires divalent cations for activity, most active with manganese Lacticaseibacillus casei
Mn2+ requires divalent cations for activity, most active with manganese Stenotrophomonas maltophilia
Mn2+ requires divalent cations for activity, most active with manganese Alteromonas sp.
additional information the enzyme requires divalent cations for activity Lactococcus lactis
additional information OPAA-2 has a conserved binuclear metal center Alteromonas sp.
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
Zn2+ interaction with amino acid residues D209, D220, H284, E313 and E327, overview Pyrococcus furiosus
Zn2+ requires divalent cations for activity, most active with zinc Lactobacillus delbrueckii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
 ?
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

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

Reaction

Reaction Comment Organism Reaction ID
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
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

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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.
10
-
 at 30°C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP Homo sapiens
30
-
 at 55°C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP Pyrococcus furiosus
1950
-
-
 Alteromonas sp.

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Pro + H2O
-
 Pyrococcus furiosus Met + Pro
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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. ?
-
 ?
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 ?
-
 ?
additional information the enzyme from guinea pig brain can also cleave substrates without a prolyl residue Cavia porcellus ?
-
 ?
additional information the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue Lacticaseibacillus casei ?
-
 ?
additional information the enzyme is also active with diisopropyl phosphorofluoridate, an organophosphorus nerve reagent Homo sapiens ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
additional information the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue Lacticaseibacillus casei IFPL 731 ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Homo sapiens
dimer
-
 Stenotrophomonas maltophilia
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
monomer
-
 Lactococcus lactis
monomer
-
 Lacticaseibacillus casei
monomer
-
 Alteromonas sp.

Synonyms

Synonyms Comment Organism
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
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
OPAA-2
-
 Alteromonas sp.
organophosphorus acid anhydrolase
-
 Alteromonas sp.
PepQ
-
 Lactobacillus delbrueckii
Pfprol
-
 Pyrococcus furiosus
prolidase
-
 Cavia porcellus
prolidase
-
 Homo sapiens
prolidase
-
 Pyrococcus furiosus
prolidase
-
 Lactococcus lactis
prolidase
-
 Lacticaseibacillus casei
prolidase
-
 Lactobacillus delbrueckii
prolidase
-
 Stenotrophomonas maltophilia
prolidase
-
 Alteromonas sp.
proline iminopeptidase
-
 Homo sapiens
proline iminopeptidase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 little activity remaining after 6 h Pyrococcus furiosus
80
-
 loss of 50% activity after 6 h Pyrococcus furiosus
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

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

General Information

General Information Comment Organism
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
metabolism the enzyme is important in the collagen metabolism, overview Homo sapiens
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.